Hiv Gp120 Crystal Structure and Its Use to Identify Immunogens

ABSTRACT

The present disclosure relates to stabilized forms of the HIV gp120 envelope protein in complex with the broadly neutralizing CD4-binding site antibody b12, to crystalline forms of the stabilized forms of the HIV gp120 envelope protein in complex with the broadly neutralizing CD4-binding site antibody b12, and to the high resolution structure obtained from these crystals by X-ray diffraction methods. Methods for identifying immunogenic polypeptides based on these structures are also disclosed.

CROSS REFERENCE TO RELATED APPLICATION

This application claims the benefit of U.S. Provisional Application No. 60/713,725, filed Sep. 6, 2005; U.S. Provisional Application No. 60/729,878, filed Oct. 24, 2005; U.S. Provisional Application No. 60/731,627, filed Oct. 28, 2005; and U.S. Provisional Application No. 60/832,458, filed Jul. 20, 2006. All of the provisional applications are incorporated by reference herein in their entirety.

FIELD OF THE DISCLOSURE

The present disclosure relates to stabilized forms of human immunodeficiency virus gp120 envelope protein, specifically to crystalline forms of gp120 in contact with the broadly neutralizing antibody b12, high resolution structures obtained from these crystals, and use thereof.

BACKGROUND

The primary immunologic abnormality resulting from infection by human immunodeficiency virus (HIV) is the progressive depletion and functional impairment of T lymphocytes expressing the CD4 cell surface glycoprotein. The loss of CD4 helper/inducer T cell function probably underlies the profound defects in cellular and humoral immunity leading to the opportunistic infections and malignancies characteristic of the acquired immunodeficiency syndrome (AIDS) (Lane et al., Ann. Rev. Immunol. 3:477, 1985). Studies of HIV-I infection of fractionated CD4 and CD8 T cells from normal donors and AIDS patients have revealed that depletion of CD4 T cells results from the ability of HIV-I to selectively infect, replicate in, and ultimately destroy this T lymphocyte subset (Klatzmann et al., Science 225:59, 1984). The possibility that CD4 itself is an essential component of the cellular receptor for HIV-I was first indicated by the observation that monoclonal antibodies directed against CD4 block HIV-I infection and syncytia induction (Dalgleish et al., Nature 312:767, 1984; McDougal et al., J. Immunol 135:3151, 1985). This hypothesis has been confirmed by the demonstration that a molecular complex forms between CD4 and the major envelope glycoprotein of HIV-I (McDougal et al., Science 231:382, 1986)

The major envelope protein of HIV-I is a glycoprotein of approximately 160 kD (gp160). During infection proteases of the host cell cleave gp160 into gp120 and gp41. gp41 is an integral membrane protein, while gp120 protrudes from the mature virus. Together gp120 and gp41 make up the HIV envelope spike.

The HIV envelope spike mediates binding to receptors and virus entry (Wyatt and Sodroski, Science 280:188, 1998). The spike is trimeric and composed of three gp120 exterior and three gp41 transmembrane envelope glycoproteins. CD4 binding to gp120 in the spike induces conformational changes that allow binding to a coreceptor, either CCR5 or CXCR4, which is required for viral entry (Dalgleish et al., Nature 312:763, 1984; Sattentau and Moore, J. Exp. Med. 174:407, 1991; Feng at al., Science 272:872, 1996; Wu et al., Nature 384:179, 1996; Trkola et al., Nature 384:184, 1996).

The mature gp120 glycoprotein is approximately 470-490 amino acids long depending on the HIV strain of origin. N-linked glycosylation at approximately 20-25 sites makes up nearly half of the mass of the molecule. Sequence analysis shows that the polypeptide is composed of five conserved regions (C1-C5) and five regions of high variability (V1-V5).

With the number of individuals infected by HIV-I approaching 1% of the world's population, an effective vaccine is urgently needed. An enveloped virus, HIV-I hides from humoral recognition behind a protective lipid bilayer. An available viral target for neutralizing antibodies is the envelope spike. Genetic, immunologic and structural studies of the HIV-I envelope glycoproteins have revealed extraordinary diversity as well as multiple overlapping mechanisms of humoral evasion, including self-masquerading glycan, immunodominant variable loops, and conformational masking. These evolutionarily honed barriers of diversity and evasion have confounded traditional means of vaccine development. It is believed that immunization with effectively immunogenic HIV gp120 envelope glycoprotein can elicit a neutralizing response directed against gp120, and thus HIV. The need exists for immunogens that are capable of eliciting an immunogenic response in a suitable subject. In order to be effective, the antibodies raised must be capable of neutralizing a broad range of HIV strains and subtypes.

SUMMARY OF THE DISCLOSURE

Disclosed herein are gp120 polypeptides and nucleic acid molecules encoding gp120 polypeptides, which are useful to induce an immunogenic response to a lentivirus, such as SIV or HIV (for example HIV-I and HIV-II) in a subject. In some examples, the gp120 polypeptide is a stabilized in a CD4 binding conformation. In some examples, the outer-domain of the gp120 polypeptide is stabilized in a CD4 binding conformation. Immunogenic compositions containing a therapeutically effective amount of gp120 polypeptides and nucleic acid molecules encoding gp120 polypeptides also are disclosed. Also disclosed are methods for eliciting and/or enhancing an immune response in a subject, for example by administering an immunogenic composition.

Crystalline forms of the gp120 envelope protein in complex with a broadly neutralizing CD4-binding site antibody are disclosed, as are atomic coordinates of gp120 polypeptides obtained from these crystals. In some examples, the crystalline form of a gp120 is crystallized in contact with a neutralizing antibody, which in one example, is a CD4-binding site antibody. In some examples, the antibody is b12. Also provided by this disclosure is a machine-readable data storage medium including a data storage material encoded with machine-readable data corresponding to the coordinates of the crystal structures disclosed herein. A computer system is disclosed for displaying the coordinate data from these crystal structures of gp120, such as the atomic positions, surface, domain, or region of the gp120 polypeptide. In several embodiments, methods are disclosed for identifying immunogens based on these structures.

The foregoing and other objects, features, and advantages of the invention will become more apparent from the following detailed description, which proceeds with reference to the accompanying figures.

BRIEF DESCRIPTION OF THE DRAWINGS

FIG. 1A is a set of computer generated images and plots of the on-rates of antibodies and CD4 as a function of entropy. FIG. 1A is a graphic representation of an atomic structure of a stabilized form of gp120. The inset panels show the electron density of specific stabilizing mutations of gp120. FIG. 1B is a graphic representation of the unliganded structure of SIV showing the positions of disulfide bonds as hatched lines. FIG. 1C is a plot of the on-rate of two CD4 induced antibodies binding gp120 as a function of −TΔS. FIG. 1D is a plot of the on-rate of CD4 binding gp120 as a function of −TΔS.

FIG. 2 is a set of computer generated images of an atomic structure of a stabilized form of gp120 in complex with the broadly neutralizing antibody b12. At left is a ribbon diagram of the structure, while at right is a space filling model of the structure of the gp120 with the side chains of b12 in contact with the gp120 molecule shown as sticks. The structure was solved at 2.3 Å by molecular replacement using the Fab portion of the b12 structure. The initial molecular replacement solution allowed the outer domain of gp120 to be placed, and iterative refinement and model building allowed portions of the less ordered inner domain and bridging sheet to be defined.

FIG. 3 is a set of computer generated images showing the atomic structure of unliganded SIV gp120, a stabilized form of HIV gp120 as it would be in complex with the broadly neutralizing antibody b12, and a stabilized form of HIV gp120 as it would be in complex with CD4.

FIG. 4 is a set of computer generated images of the atomic structures of stabilized forms of gp120 as they would be in complex with the broadly neutralizing antibody b12 and in complex with CD4. FIG. 4A depicts the stabilized form of gp120 as a molecular surface model. The light colored patches on the molecular surfaces of the gp120 models show the surface in contact with b12 and CD4 respectively; b12 and CD4 have been removed clarity. The Table at bottom summarizes the total surface are buried by the formation of the CD4:gp120 complex and the b12:gp120 complex. This figure shows that the binding surfaces on gp120 while overlapping are not identical. FIG. 4B depicts stabilized forms of gp120 as ribbon diagrams. The panel at left shows the structure of gp120 as it would be in complex with CD4, the panel at right shows the conformation of gp120 as it would be in complex with the b12 antibody. Comparison of these two structures shows that the outer domain of these two structures is relatively rigid in both complexes, while the inner domain is more flexible in the b12 complex than in the CD4 complex. FIG. 4C is a representation of the CD4 binding loop of gp120 (dark) in contact with b12 (light, left) and CD4 (light, right). The CD4 binding loop appears to make more significant contacts with the b12 antibody than with CD4. FIG. 4D is a molecular surface representation of the atomic structure of stabilized forms of gp120 depicting the different modes of CD4 and b12 binding. b12 makes contacts on either side of the CD4 binding loop, while CD4 predominately binds to a single side.

FIG. 5 is a set of diagrams generated by the program ligplot showing the detailed molecular interactions between a stabilized form of gp120 and the heavy chain of the b12 antibody. FIG. 5A is a ligplot diagram showing the specific molecular interactions between the CDR H1 of b12 and gp120. FIG. 5B is a ligplot diagram showing the specific molecular interactions between the CDR H2 of b12 and gp120. FIG. 5C is a ligplot diagram showing the specific molecular interactions between the CDR H3 of b12 and gp120. FIG. 5D is a ligplot diagram showing the specific molecular interactions between b12 and the CD4 binding loop of gp120.

FIG. 6 is a computer generated image of the atomic structure of a stabilized form of gp120 as it would be in complex with the broadly neutralizing antibody b12. The structure is shown as a ribbon diagram. The Table at bottom summarizes the contact surface area buried for various elements of gp120 of secondary structure.

FIG. 7 is a computer generated image showing a molecular surface representation of the atomic structure of a stabilized form of gp120 in complex with the broadly neutralizing antibody b12. The contacting residues of gp120 and b12 are shown as sticks. The Table at bottom shows several important b12 contacts and the surface area buried by these contacts. The b12 residue numbering is given in the Kabat numbering convention.

FIG. 8 is a proposed model of the binding of b12 and CD4 to the gp120 trimer.

FIG. 9 is a diagram of the secondary structure and amino acid sequence of the b12 antibody. FIG. 9A is the heavy chain. FIG. 9 b is the light chain. Kabat numbering can be determined.

FIG. 10 is a table (supplemental Table 1) with tabulated data for the characterization of stabilized forms of stabilizing gp120 by x-ray crystallography, isothermal titration calorimetry and surface plasmon resonance.

FIG. 11 contains two tables (supplemental Table 2 and supplemental Table 3) with tabulated data for selected forms of gp120, both wildtype and stabilized. Supplemental Table 2 shows selected forms of gp120 correlated to the number of non-naturally occurring disulfide linkages, and the percentage of folded molecules available in solution. For example, mutant C2S2 has one introduced disulfide linkage and is 100% folded in solution. Supplemental Table 3 shows the thermodynamic parameters of CD4 binding to selected mutants.

FIG. 12 contains two tables (supplemental Table 4a and supplemental Table 4b) with tabulated data for selected forms of gp120, both wildtype and stabilized, binding to CD4 or various antibodies. Supplemental Table 4a shows the on-rates off-rates and K_(d) for CD4 and two CD4i antibodies binding to selected forms of gp120. Supplemental Table 4b shows the on-rates off-rates and K_(d) for CD4BS and carbohydrate binding antibodies binding to selected forms of gp120.

FIG. 13 is tabulated date and plots of neutralization data obtained from rabbits immunized with four prime cycles of BSA or the indicated gp120. FIGS. 13A and 13B are tables showing the percent neutralization of the indicated viruses by sera obtained from rabbits immunized with the indicated stabilized forms of gp120, followed by immunization with a stabilized gp140 trimer. FIG. 13C is tabulated neutralization data from sera obtained from the indicated animals. The data show the effects of various peptides on the neutralization of HIV isolate YU2.SG3. This data demonstrates that the YU V3 peptide blocks neutralization of HIV isolate YU2.SG3 by antibodies produced by the boost prime immunization scheme described in Example 9. FIGS. 13D-13M are graphical representations of the data shown in FIG. 13C.

SEQUENCE LISTING AND NOMENCLATURE

The nucleic and amino acid sequences listed in the accompanying sequence listing are shown using standard letter abbreviations for nucleotide bases, and three letter code for amino acids, as defined in 37 C.F.R. 1.822. Only one strand of each nucleic acid sequence is shown, but the complementary strand is understood as included by any reference to the displayed strand.

SEQ ID NO: 1 is the amino acid sequence of a stabilized form of a gp120 polypeptide.

Mutant location M95W T257S W96C I109C T123C K231C K231C S375W A433M V275C Q428C G431C E267C E268C Mutant Name New name C2 C3 C1S1 S2 S3 S4 S5 WT core WT core 2a C2 x 4-0 C2S5 x x 4a C2S2 x x 4b C2S4 x x 4c C2S3 x x 5mut C12S1 x x 6a C123S1 x x x 6b C2S24 x x x 8a C123S14 x x x x 8b C123S12 x x x x 9a C23S234 x x x x x 8c C2S234 x x x x 10a C123S124 x x x x x 9b C12S134 x x x x 10c C123S134 x x x x x 9c C12S123 x x x x 10b C123S123 x x x x x 11a C12S1234 x x x x x

DETAILED DESCRIPTION I. Terms

Unless otherwise noted, technical terms are used according to conventional usage. Definitions of common terms in molecular biology can be found in Benjamin Lewin, Genes V, published by Oxford University Press, 1994 (ISBN 0-19-854287-9); Kendrew et al. (eds.), The Encyclopedia of Molecular Biology, published by Blackwell Science Ltd., 1994 (ISBN 0-632-02182-9); and Robert A. Meyers (ed.), Molecular Biology and Biotechnology: a Comprehensive Desk Reference, published by VCH Publishers, Inc., 1995 (ISBN 1-56081-569-8). Terms describing protein structure and structural elements of proteins can be found in Creighton, Proteins, Structures and Molecular Properties, W.H. Freeman & Co., New York, 1993 (ISBN 0-717-7030) which is incorporated by reference herein in its entirety.

Unless otherwise explained, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure belongs. The singular terms “a,” “an,” and “the” include plural referents unless context clearly indicates otherwise. Similarly, the word “or” is intended to include “and” unless the context clearly indicates otherwise. It is further to be understood that all base sizes or amino acid sizes, and all molecular weight or molecular mass values, given for nucleic acids or polypeptides are approximate, and are provided for description. Although methods and materials similar or equivalent to those described herein can be used in the practice or testing of this disclosure, suitable methods and materials are described below. The term “comprises” means “includes.” The abbreviation, “e.g.” is derived from the Latin exempli gratia, and is used herein to indicate a non-limiting example. Thus, the abbreviation “e.g.” is synonymous with the term “for example.”

All publications, patent applications, patents, and other references mentioned herein are incorporated by reference in their entirety. In case of conflict, the present specification, including explanations of terms, will control. In addition, all the materials, methods, and examples are illustrative and not intended to be limiting. In order to facilitate review of the various embodiments of the disclosure, the following explanations of specific terms are provided:

Adjuvant: A vehicle used to enhance antigenicity; such as a suspension of minerals (alum, aluminum hydroxide, aluminum phosphate) on which antigen is adsorbed; or water-in-oil emulsion in which antigen solution is emulsified in oil (MF-59, Freund's incomplete adjuvant), sometimes with the inclusion of killed mycobacteria (Freund's complete adjuvant) to further enhance antigenicity (inhibits degradation of antigen and/or causes influx of macrophages). Adjuvants also include immunostimulatory molecules, such as cytokines, costimulatory molecules, and for example, immunostimulatory DNA or RNA molecules, such as CpG oligonucleotides.

Administration: The introduction of a composition into a subject by a chosen route. For example, if the chosen route is intravenous, the composition is administered by introducing the composition into a vein of the subject.

Antibody: A polypeptide substantially encoded by an immunoglobulin gene or immunoglobulin genes, or fragments thereof, which specifically binds and recognizes an analyte (antigen) such as gp120 or an antigenic fragment of gp120. Immunoglobulin genes include the kappa, lambda, alpha, gamma, delta, epsilon and mu constant region genes, as well as the myriad immunoglobulin variable region genes.

Antibodies exist, for example as intact immunoglobulins and as a number of well characterized fragments produced by digestion with various peptidases. For instance, Fabs, Fvs, and single-chain Fvs (SCFvs) that bind to gp120 or fragments of gp120 would be gp120-specific binding agents. This includes intact immunoglobulins and the variants and portions of them well known in the art, such as Fab′ fragments, F(ab)′₂ fragments, single chain Fv proteins (“scFv”), and disulfide stabilized Fv proteins (“dsFv”). A scFv protein is a fusion protein in which a light chain variable region of an immunoglobulin and a heavy chain variable region of an immunoglobulin are bound by a linker, while in dsFvs, the chains have been mutated to introduce a disulfide bond to stabilize the association of the chains. The term also includes genetically engineered forms such as chimeric antibodies (such as humanized murine antibodies), heteroconjugate antibodies such as bispecific antibodies). See also, Pierce Catalog and Handbook, 1994-1995 (Pierce Chemical Co., Rockford, Ill.); Kuby, J., Immunology, 3^(rd) Ed., W.H. Freeman & Co., New York, 1997.

Antibody fragments are defined as follows: (1) Fab, the fragment which contains a monovalent antigen-binding fragment of an antibody molecule produced by digestion of whole antibody with the enzyme papain to yield an intact light chain and a portion of one heavy chain; (2) Fab′, the fragment of an antibody molecule obtained by treating whole antibody with pepsin, followed by reduction, to yield an intact light chain and a portion of the heavy chain; two Fab′ fragments are obtained per antibody molecule; (3) (Fab′)2, the fragment of the antibody obtained by treating whole antibody with the enzyme pepsin without subsequent reduction; (4) F(ab′)2, a dimer of two Fab′ fragments held together by two disulfide bonds; (5) Fv, a genetically engineered fragment containing the variable region of the light chain and the variable region of the heavy chain expressed as two chains; and (6) single chain antibody (“SCA”), a genetically engineered molecule containing the variable region of the light chain, the variable region of the heavy chain, linked by a suitable polypeptide linker as a genetically fused single chain molecule. The term “antibody,” as used herein, also includes antibody fragments either produced by the modification of whole antibodies or those synthesized de novo using recombinant DNA methodologies.

Typically, a naturally occurring immunoglobulin has heavy (H) chains and light (L) chains interconnected by disulfide bonds. There are two types of light chain, lambda (λ) and kappa (κ). There are five main heavy chain classes (or isotypes) which determine the functional activity of an antibody molecule: IgM, IgD, IgG, IgA and IgE.

Each heavy and light chain contains a constant region and a variable region, (the regions are also known as “domains”). In combination, the heavy and the light chain variable regions specifically bind the antigen. Light and heavy chain variable regions contain a “framework” region interrupted by three hypervariable regions, also called “complementarity-determining regions” or “CDRs.” The extent of the framework region and CDRs have been defined (see, Kabat et al., Sequences of Proteins of Immunological Interest, U.S. Department of Health and Human Services, 1991, which is hereby incorporated by reference). The Kabat database is now maintained online. The sequences of the framework regions of different light or heavy chains are relatively conserved within a species. The framework region of an antibody, that is the combined framework regions of the constituent light and heavy chains, serves to position and align the CDRs in three-dimensional space.

The CDRs are primarily responsible for binding to an epitope of an antigen. The CDRs of each chain are typically referred to as CDR1, CDR2, and CDR3, numbered sequentially starting from the N-terminus, and are also typically identified by the chain in which the particular CDR is located. Thus, a V_(H) CDR3 is located in the variable domain of the heavy chain of the antibody in which it is found, whereas a V_(L) CDR1 is the CDR 1 from the variable domain of the light chain of the antibody in which it is found. Light chain CDRs are sometimes referred to as CDR L1, CDR L2, and CDR L3. Heavy chain CDRs are sometimes referred to as CDR H1, CDR H2, and CDR H3.

References to “V_(H)” or “V_(H)” refer to the variable region of an immunoglobulin heavy chain, including that of an Fv, scFv, dsFv or Fab. References to “V_(L)” or “VL” refer to the variable region of an immunoglobulin light chain, including that of an Fv, scFv, dsFv or Fab.

A “monoclonal antibody” is an antibody produced by a single clone of B-lymphocytes or by a cell into which the light and heavy chain genes of a single antibody have been transfected. Monoclonal antibodies are produced by methods known to those of skill in the art, for instance by making hybrid antibody-forming cells from a fusion of myeloma cells with immune spleen cells. These fused cells and their progeny are termed “hybridomas.” Monoclonal antibodies include humanized monoclonal antibodies.

A “humanized” immunoglobulin is an immunoglobulin including a human framework region and one or more CDRs from a non-human (such as a mouse, rat, or synthetic) immunoglobulin. The non-human immunoglobulin providing the CDRs is termed a “donor,” and the human immunoglobulin providing the framework is termed an “acceptor.” In one embodiment, all the CDRs are from the donor immunoglobulin in a humanized immunoglobulin. Constant regions need not be present, but if they are, they must be substantially identical to human immunoglobulin constant regions, such as at least about 85-90%, such as about 95% or more identical. Hence, all parts of a humanized immunoglobulin, except possibly the CDRs, are substantially identical to corresponding parts of natural human immunoglobulin sequences. A “humanized antibody” is an antibody comprising a humanized light chain and a humanized heavy chain immunoglobulin. A humanized antibody binds to the same antigen as the donor antibody that provides the CDRs. The acceptor framework of a humanized immunoglobulin or antibody may have a limited number of substitutions by amino acids taken from the donor framework. Humanized or other monoclonal antibodies can have additional conservative amino acid substitutions which have substantially no effect on antigen binding or other immunoglobulin functions. Humanized immunoglobulins can be constructed by means of genetic engineering (for example, see U.S. Pat. No. 5,585,089).

Antigenic gp120 polypeptide: An “antigenic gp120 polypeptide” includes a gp120 molecule or a portion thereof that is capable of provoking an immune response in a mammal, such as a mammal with or without an HIV infection. Administration of an antigenic gp120 polypeptide that provokes an immune response preferably leads to protective immunity against HIV.

Antigenic surface: A surface of a molecule, for example a protein such as a gp120 protein or polypeptide, capable of eliciting an immune response. An antigenic surface includes the defining features of that surface, for example the three-dimensional shape and the surface charge. An antigenic surface includes both surfaces that occur on gp120 polypeptides as well as surfaces of compounds that mimic the surface of a gp120 polypeptide (mimetics).

CD4: Cluster of differentiation factor 4 polypeptide, a T-cell surface protein that mediates interaction with the MHC class II molecule. CD4 also serves as the primary receptor site for HIV on T-cells during HIV-I infection.

The known sequence of the CD4 precursor has a hydrophobic signal peptide, an extracellular region of approximately 370 amino acids, a highly hydrophobic stretch with significant identity to the membrane-spanning domain of the class II MHC beta chain, and a highly charged intracellular sequence of 40 resides (Maddon, Cell 42:93, 1985).

The term “CD4” includes polypeptide molecules that are derived from CD4 include fragments of CD4, generated either by chemical (for example enzymatic) digestion or genetic engineering means. Such a fragment may be one or more entire CD4 protein domains. The extracellular domain of CD4 consists of four contiguous immunoglobulin-like regions (D1, D2, D3, and D4, see Sakihama et al., Proc. Natl. Acad. Sci. 92:6444, 1995; U.S. Pat. No. 6,117,655), and aminoacids 1 to 183 have been shown to be involved in gp120 binding. For instance, a binding molecule or binding domain derived from CD4 would comprise a sufficient portion of the CD4 protein to mediate specific and functional interaction between the binding fragment and a native or viral binding site of CD4. One such binding fragment includes both the D1 and D2 extracellular domains of CD4 (D1D2 is also a fragment of soluble CD4 or sCD4 which is comprised of D1 D2 D3 and D4), although smaller fragments may also provide specific and functional CD4-like binding. The gp120-binding site has been mapped to D1 of CD4.

CD4 polypeptides also include “CD4-derived molecules” which encompasses analogs (non-protein organic molecules), derivatives (chemically functionalized protein molecules obtained starting with the disclosed protein sequences) or mimetics (three-dimensionally similar chemicals) of the native CD4 structure, as well as proteins sequence variants or genetic alleles that maintain the ability to functionally bind to a target molecule.

b12 antibody: The b12 antibody is a broadly neutralizing antibody against human immunodeficiency virus type I (HIV-I). The epitope recognized by b12 overlaps the CD4 receptor-binding site (CD4BS) on gp120, see Zwick et al., J. of Virology 77: 5863-5870, 2003, herein incorporated by reference.

CD4BS antibodies: Antibodies that bind to or substantially overlap the CD4 binding surface of a gp120 polypeptide. The antibodies interfere with or prevent CD4 from binding to a gp120 polypeptide.

CD4i antibodies: Antibodies that bind to a conformation of gp120 induced by CD4 binding.

Contacting: Placement in direct physical association; includes both in solid and liquid form.

Computer readable media: Any medium or media, which can be read and accessed directly by a computer, so that the media is suitable for use in a computer system. Such media include, but are not limited to: magnetic storage media such as floppy discs, hard disc storage medium and magnetic tape; optical storage media such as optical discs or CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media.

Computer system: Hardware that can be used to analyze atomic coordinate data. The minimum hardware of a computer-based system typically comprises a central processing unit (CPU), an input device, for example a mouse, keyboard, and the like, an output device, and a data storage device. Desirably a monitor is provided to visualize structure data. The data storage device may be RAM or other means for accessing computer readable. Examples of such systems are microcomputer workstations available from Silicon Graphics Incorporated and Sun Microsystems running Unix based Windows NT or IBM OS/2 operating systems.

Degenerate variant and conservative variant: A polynucleotide encoding a polypeptide or an antibody that includes a sequence that is degenerate as a result of the genetic code. For example, a polynucleotide encoding a gp120 polypeptide or an antibody that binds gp120 that includes a sequence that is degenerate as a result of the genetic code. There are 20 natural amino acids, most of which are specified by more than one codon. Therefore, all degenerate nucleotide sequences are included as long as the amino acid sequence of the gp120 polypeptide or antibody that binds gp120 encoded by the nucleotide sequence is unchanged. Because of the degeneracy of the genetic code, a large number of functionally identical nucleic acids encode any given polypeptide. For instance, the codons CGU, CGC, CGA, CGG, AGA, and AGG all encode the amino acid arginine. Thus, at every position where an arginine is specified within a protein encoding sequence, the codon can be altered to any of the corresponding codons described without altering the encoded protein. Such nucleic acid variations are “silent variations,” which are one species of conservative variations. Each nucleic acid sequence herein that encodes a polypeptide also describes every possible silent variation. One of skill will recognize that each codon in a nucleic acid (except AUG, which is ordinarily the only codon for methionine) can be modified to yield a functionally identical molecule by standard techniques. Accordingly, each “silent variation” of a nucleic acid which encodes a polypeptide is implicit in each described sequence.

Furthermore, one of ordinary skill will recognize that individual substitutions, deletions or additions which alter, add or delete a single amino acid or a small percentage of amino acids (for instance less than 5%, in some embodiments less than 1%) in an encoded sequence are conservative variations where the alterations result in the substitution of an amino acid with a chemically similar amino acid.

Conservative amino acid substitutions providing functionally similar amino acids are well known in the art. The following six groups each contain amino acids that are conservative substitutions for one another:

1) Alanine (A), Serine (S), Threonine (T);

2) Aspartic acid (D), Glutamic acid (E);

3) Asparagine (N), Glutamine (Q);

4) Arginine (R), Lysine (K);

5) Isoleucine (I), Leucine (L), Methionine (M), Valine (V); and

6) Phenylalanine (F), Tyrosine (Y), Tryptophan (W).

Not all residue positions within a protein will tolerate an otherwise “conservative” substitution. For instance, if an amino acid residue is essential for a function of the protein, even an otherwise conservative substitution may disrupt that activity.

Epitope: An antigenic determinant. These are particular chemical groups or peptide sequences on a molecule that are antigenic, such that they elicit a specific immune response. An antibody binds a particular antigenic epitope, such as an epitope of a gp120 polypeptide.

Expression: Translation of a nucleic acid into a protein. Proteins may be expressed and remain intracellular, become a component of the cell surface membrane, or be secreted into the extracellular matrix or medium.

Expression Control Sequences: Nucleic acid sequences that regulate the expression of a heterologous nucleic acid sequence to which it is operatively linked. Expression control sequences are operatively linked to a nucleic acid sequence when the expression control sequences control and regulate the transcription and, as appropriate, translation of the nucleic acid sequence. Thus expression control sequences can include appropriate promoters, enhancers, transcription terminators, a start codon (ATG) in front of a protein-encoding gene, splicing signal for introns, maintenance of the correct reading frame of that gene to permit proper translation of mRNA, and stop codons. The term “control sequences” is intended to include, at a minimum, components whose presence can influence expression, and can also include additional components whose presence is advantageous, for example, leader sequences and fusion partner sequences. Expression control sequences can include a promoter.

A promoter is a minimal sequence sufficient to direct transcription. Also included are those promoter elements which are sufficient to render promoter-dependent gene expression controllable for cell-type specific, tissue-specific, or inducible by external signals or agents; such elements may be located in the 5′ or 3′ regions of the gene. Both constitutive and inducible promoters are included (see for example, Bitter et al., Methods in Enzymology 153:516-544, 1987). For example, when cloning in bacterial systems, inducible promoters such as pL of bacteriophage lambda, plac, ptrp, ptac (ptrp-lac hybrid promoter) and the like may be used. In one embodiment, when cloning in mammalian cell systems, promoters derived from the genome of mammalian cells (such as metallothionein promoter) or from mammalian viruses (such as the retrovirus long terminal repeat; the adenovirus late promoter; the vaccinia virus 7.5K promoter) can be used. Promoters produced by recombinant DNA or synthetic techniques may also be used to provide for transcription of the nucleic acid sequences.

A polynucleotide can be inserted into an expression vector that contains a promoter sequence which facilitates the efficient transcription of the inserted genetic sequence of the host. The expression vector typically contains an origin of replication, a promoter, as well as specific nucleic acid sequences that allow phenotypic selection of the transformed cells.

gp120: The envelope protein from Human Immunodeficiency Virus (HIV). The envelope protein is initially synthesized as a longer precursor protein of 845-870 amino acids in size, designated gp160. Gp160 forms a homotrimer and undergoes glycosylation within the Golgi apparatus. It is then cleaved by a cellular protease into gp120 and gp41. Gp41 contains a transmembrane domain and remains in a trimeric configuration; it interacts with gp120 in a non-covalent manner. Gp120 contains most of the external, surface-exposed, domains of the envelope glycoprotein complex, and it is gp120 which binds both to the cellular CD4 receptor and to the cellular chemokine receptors (such as CCR5).

The mature gp120 wildtype polypeptides have about 500 amino acids in the primary sequence. Gp120 is heavily N-glycosylated giving rise to an apparent molecular weight of 120 kD. The polypeptide is comprised of five conserved regions (C1-C5) and five regions of high variability (V1-V5). Exemplary sequence of wt gp160 polypeptides are shown on GENBANK, for example accession numbers AAB05604 and AAD12142

The gp120 core has a unique molecular structure, which comprises two domains: an “inner” domain (which faces gp41) and an “outer” domain (which is mostly exposed on the surface of the oligomeric envelope glycoprotein complex). The two gp120 domains are separated by a “bridging sheet” that is not part of either domain. The gp120 core comprises 25 beta strands, 5 alpha helices, and 10 defined loop segments.

“Stabilized gp120” is a form of gp120 polypeptide from HIV-1, characterized by an increase in T_(m) over the wild type gp120. In some examples the gp120 is stabilized by the replacement of at least two amino acids of gp120 with cysteines such that a disulfide bond can form, wherein the gp120 protein has a T_(m) of greater than about 53.8° C. The stabilized gp120 mutants may contain amino acid substitutions that fill cavities present in the core of native gp120. The stabilized gp120 can bind CD4. Stabilized forms of gp120 may include forms that have synthetic amino acids. Several exemplary stabilized gp120 proteins are disclosed herein.

Gp120 polypeptides also include “gp120-derived molecules” which encompasses analogs (non-protein organic molecules), derivatives (chemically functionalized protein molecules obtained starting with the disclosed protein sequences) or mimetics (three-dimensionally similar chemicals) of the native gp120 structure, as well as proteins sequence variants (such as mutants), genetic alleles, fusions proteins of gp120, or combinations thereof.

The third variable region referred to herein as the V3 loop is a loop of about 35 amino acids critical for the binding of the co-receptor and determination of which of the co-receptors will bind. In certain examples the V3 loop comprises residues 296-331.

The numbering used in gp120 polypeptides disclosed herein is relative to the HXB2 numbering scheme as set forth in Numbering Positions in HIV Relative to HXB2CG Bette Korber et al, Human Retroviruses and AIDS 1998: A Compilation and Analysis of Nucleic Acid and Amino Acid Sequences. Korber B, Kuiken C L, Foley B, Hahn B, McCutchan F, Mellors J W, and Sodroski J, Eds. Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, N. Mex. which is incorporated by reference herein in its entirety.

Heavy atom derivatization: A method of producing a chemically modified form of a protein crystal, for example a crystal containing gp120. In practice, a crystal is soaked in a solution containing heavy metal atom salts, or organometallic compounds, such as lead chloride, gold thiomalate, thimerosal or uranyl acetate, which can diffuse through the solvent channels of the crystal and bind the surface of the protein. The location(s) of the bound heavy metal atom(s) can be determined by X-ray diffraction analysis of the soaked crystal. This information, in turn, is used to generate the phase information used to construct three-dimensional structure of the enzyme (see Blundel and Johnson, Protein Crystallography, Academic Press (1976).

Host cells: Cells in which a vector can be propagated and its DNA expressed. The cell may be prokaryotic or eukaryotic. The term also includes any progeny of the subject host cell. It is understood that all progeny may not be identical to the parental cell since there may be mutations that occur during replication. However, such progeny are included when the term “host cell” is used.

In silico: A process performed virtually within a computer. For example, using a computer, a virtual compound can be screened for surface similarity or conversely surface complementarity to a virtual representation of the atomic positions at least a portion of a gp120 polypeptide, for example as stabilized gp120, such as defined in Table 1.

Immune response: A response of a cell of the immune system, such as a B cell, T cell, or monocyte, to a stimulus. In one embodiment, the response is specific for a particular antigen (an “antigen-specific response”). In one embodiment, an immune response is a T cell response, such as a CD4+ response or a CD8+ response. In another embodiment, the response is a B cell response, and results in the production of specific antibodies.

Immunogenic peptide: A peptide which comprises an allele-specific motif or other sequence, such as an N-terminal repeat, such that the peptide will bind an MHC molecule and induce a cytotoxic T lymphocyte (“CTL”) response, or a B cell response (for example antibody production) against the antigen from which the immunogenic peptide is derived.

In one embodiment, immunogenic peptides are identified using sequence motifs or other methods, such as neural net or polynomial determinations known in the art. Typically, algorithms are used to determine the “binding threshold” of peptides to select those with scores that give them a high probability of binding at a certain affinity and will be immunogenic. The algorithms are based either on the effects on MHC binding of a particular amino acid at a particular position, the effects on antibody binding of a particular amino acid at a particular position, or the effects on binding of a particular substitution in a motif-containing peptide. Within the context of an immunogenic peptide, a “conserved residue” is one which appears in a significantly higher frequency than would be expected by random distribution at a particular position in a peptide. In one embodiment, a conserved residue is one where the MHC structure may provide a contact point with the immunogenic peptide. In one specific non-limiting example, an immunogenic polypeptide includes a region of gp120, or a fragment thereof.

Immunogenic composition: A composition comprising an immunogenic peptide that induces a measurable CTL response against virus expressing the immunogenic peptide, or induces a measurable B cell response (such as production of antibodies) against the immunogenic peptide. In one example an “immunogenic composition” is composition comprising a gp120 polypeptide that induces a measurable CTL response against virus expressing gp120 polypeptide, or induces a measurable B cell response (such as production of antibodies) against a gp120 polypeptide. It further refers to isolated nucleic acids encoding an immunogenic peptide, such as a nucleic acid that can be used to express the gp120 polypeptide (and thus be used to elicit an immune response against this polypeptide).

For in vitro use, an immunogenic composition may consist of the isolated protein, peptide epitope, or nucleic acid encoding the protein, or peptide epitope. For in vivo use, the immunogenic composition will typically comprise the protein or immunogenic peptide in pharmaceutically acceptable carriers, and/or other agents. Any particular peptide, such as a gp120 polypeptide, or nucleic acid encoding the polypeptide, can be readily tested for its ability to induce a CTL or B cell response by art-recognized assays. Immunogenic compositions can include adjuvants, which are well known to one of skill in the art.

Immunologically reactive conditions: Includes reference to conditions which allow an antibody raised against a particular epitope to bind to that epitope to a detectably greater degree than, and/or to the substantial exclusion of, binding to substantially all other epitopes. Immunologically reactive conditions are dependent upon the format of the antibody binding reaction and typically are those utilized in immunoassay protocols or those conditions encountered in vivo. The immunologically reactive conditions employed in the methods are “physiological conditions” which include reference to conditions (such as temperature, osmolarity, pH) that are typical inside a living mammal or a mammalian cell. While it is recognized that some organs are subject to extreme conditions, the intra-organismal and intracellular environment is normally about pH 7 (such as from pH 6.0 to pH 8.0, more typically pH 6.5 to 7.5), contains water as the predominant solvent, and exists at a temperature above 0° C. and below 50° C. Osmolarity is within the range that is supportive of cell viability and proliferation.

Immunotherapy: A method of evoking an immune response against a virus based on their production of target antigens. Immunotherapy based on cell-mediated immune responses involves generating a cell-mediated response to cells that produce particular antigenic determinants, while immunotherapy based on humoral immune responses involves generating specific antibodies to virus that produce particular antigenic determinants.

Inhibiting or treating a disease: Inhibiting the full development of a disease or condition, for example, in a subject who is at risk for a disease such as acquired immune deficiency syndrome (AIDS), AIDS related conditions, HIV-I infection, or combinations thereof. “Treatment” refers to a therapeutic intervention that ameliorates a sign or symptom of a disease or pathological condition after it has begun to develop. The term “ameliorating,” with reference to a disease or pathological condition, refers to any observable beneficial effect of the treatment. The beneficial effect can be evidenced, for example, by a delayed onset of clinical symptoms of the disease in a susceptible subject, a reduction in severity of some or all clinical symptoms of the disease, a slower progression of the disease, a reduction in the number of metastases, an improvement in the overall health or well-being of the subject, or by other parameters well known in the art that are specific to the particular disease. A “prophylactic” treatment is a treatment administered to a subject who does not exhibit signs of a disease or exhibits only early signs for the purpose of decreasing the risk of developing pathology.

Isolated: An “isolated” biological component (such as a nucleic acid, peptide or protein) has been substantially separated, produced apart from, or purified away from other biological components in the cell of the organism in which the component naturally occurs, such as, other chromosomal and extrachromosomal DNA and RNA, and proteins. Nucleic acids, peptides and proteins which have been “isolated” thus include nucleic acids and proteins purified by standard purification methods. The term also embraces nucleic acids, peptides, and proteins prepared by recombinant expression in a host cell as well as chemically synthesized nucleic acids.

K_(d): The dissociation constant for a given interaction, such as a polypeptide ligand interaction. For example, for the bimolecular interaction of b12 and gp120 it is the concentration of the individual components of the bimolecular interaction divided by the concentration of the complex.

Leukocyte: Cells in the blood, also termed “white cells,” that are involved in defending the body against infective organisms and foreign substances. Leukocytes are produced in the bone marrow. There are 5 main types of white blood cell, subdivided between 2 main groups: polymorphonuclear leukocytes (neutrophils, eosinophils, basophils) and mononuclear leukocytes (monocytes and lymphocytes).

Ligand: Any molecule which specifically binds a protein, such as a gp120 protein, and includes, inter alia, antibodies that specifically bind a gp120 protein. In alternative embodiments, the ligand is a protein or a small molecule (one with a molecular weight less than 6 kiloDaltons).

Mimetic: A molecule (such as an organic chemical compound) that mimics the activity of an agent, such as the activity of a gp120 protein, for example by inducing an immune response to gp120. Peptidomimetic and organomimetic embodiments are within the scope of this term, whereby the three-dimensional arrangement of the chemical constituents of such peptido- and organomimetics mimic the three-dimensional arrangement of the peptide backbone and component amino acid side chains in the peptide, resulting in such peptido- and organomimetics of the peptides having substantial specific activity. For computer modeling applications, a pharmacophore is an idealized, three-dimensional definition of the structural requirements for biological activity. Peptido- and organomimetics can be designed to fit each pharmacophore with computer modeling software (using computer assisted drug design or CADD). See Walters, “Computer-Assisted Modeling of Drugs”, in Klegerman & Groves, eds., 1993, Pharmaceutical Biotechnology, Interpharm Press: Buffalo Grove, Ill., pp. 165-174 and Principles of Pharmacology (ed. Munson, 1995), chapter 102 for a description of techniques used in computer assisted drug design.

Molecular Replacement: A method that involves generating a preliminary model, such as a model of a gp120 polypeptide, whose structure coordinates are unknown, by orienting and positioning a molecule whose structure coordinates are known (such as coordinates from Table 1) within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown molecule (see Lattman, Methods in Enzymology, 115:55-77, 1985; Rossmann, ed., “The Molecular Replacement Method”, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York, 1972). Using the structure coordinates of gp120, such as a stabilized gp120 provided herein; molecular replacement may be used to determine the structure coordinates of a crystalline mutant or homologue of gp120, a different crystal form of gp120, or gp120 in complex with another molecule, such as an antibody, cell surface receptor, or combination thereof.

Naturally Occurring Amino Acids: L-isomers of the naturally occurring amino acids. The naturally occurring amino acids are glycine, alanine, valine, leucine, isoleucine, serine, methionine, threonine, phenylalanine, tyrosine, tryptophan, cysteine, proline, histidine, aspartic acid, asparagine, glutamic acid, glutamine, gamma.-carboxyglutamic acid, arginine, ornithine and lysine. Unless specifically indicated, all amino acids referred to in this application are in the L-form. “Synthetic amino acids” refers to amino acids that are not naturally found in proteins. Examples of synthetic amino acids used herein, include racemic mixtures of selenocysteine and selenomethionine. In addition, unnatural amino acids include the D or L forms of nor-leucine, para-nitrophenylalanine, homophenylalanine, para-fluorophenylalanine, 3-amino-2-benzylpropionic acid, homoarginine, and D-phenylalanine. The term “positively charged amino acid” refers to any naturally occurring or synthetic amino acid having a positively charged side chain under normal physiological conditions. Examples of positively charged naturally occurring amino acids are arginine, lysine and histidine. The term “negatively charged amino acid” refers to any naturally occurring or synthetic amino acid having a negatively charged side chain under normal physiological conditions. Examples of negatively charged naturally occurring amino acids are aspartic acid and glutamic acid. The term “hydrophobic amino acid” refers to any amino acid having an uncharged, nonpolar side chain that is relatively insoluble in water. Examples of naturally occurring hydrophobic amino acids are alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan and methionine. The term “hydrophilic amino acid” refers to any amino acid having an uncharged, polar side chain that is relatively soluble in water. Examples of naturally occurring hydrophilic amino acids are serine, threonine, tyrosine, asparagine, glutamine, and cysteine.

Nucleic acid: A polymer composed of nucleotide units (ribonucleotides, deoxyribonucleotides, related naturally occurring structural variants, and synthetic non-naturally occurring analogs thereof) linked via phosphodiester bonds, related naturally occurring structural variants, and synthetic non-naturally occurring analogs thereof. Thus, the term includes nucleotide polymers in which the nucleotides and the linkages between them include non-naturally occurring synthetic analogs, such as, for example and without limitation, phosphorothioates, phosphoramidates, methyl phosphonates, chiral-methyl phosphonates, 2-O-methyl ribonucleotides, peptide-nucleic acids (PNAs), and the like. Such polynucleotides can be synthesized, for example, using an automated DNA synthesizer. The term “oligonucleotide” typically refers to short polynucleotides, generally no greater than about 50 nucleotides. It will be understood that when a nucleotide sequence is represented by a DNA sequence (i.e., A, T, G, C), this also includes an RNA sequence (i.e., A, U, G, C) in which “U” replaces “T.”

“Nucleotide” includes, but is not limited to, a monomer that includes a base linked to a sugar, such as a pyrimidine, purine or synthetic analogs thereof, or a base linked to an amino acid, as in a peptide nucleic acid (PNA). A nucleotide is one monomer in a polynucleotide. A nucleotide sequence refers to the sequence of bases in a polynucleotide. A gp120 polynucleotide is a nucleic acid encoding a gp120 polypeptide.

Conventional notation is used herein to describe nucleotide sequences: the left-hand end of a single-stranded nucleotide sequence is the 5′-end; the left-hand direction of a double-stranded nucleotide sequence is referred to as the 5′-direction. The direction of 5′ to 3′ addition of nucleotides to nascent RNA transcripts is referred to as the transcription direction. The DNA strand having the same sequence as an mRNA is referred to as the “coding strand;” sequences on the DNA strand having the same sequence as an mRNA transcribed from that DNA and which are located 5′ to the 5′-end of the RNA transcript are referred to as “upstream sequences;” sequences on the DNA strand having the same sequence as the RNA and which are 3′ to the 3′ end of the coding RNA transcript are referred to as “downstream sequences.”

“cDNA” refers to a DNA that is complementary or identical to an mRNA, in either single stranded or double stranded form.

“Encoding” refers to the inherent property of specific sequences of nucleotides in a polynucleotide, such as a gene, a cDNA, or an mRNA, to serve as templates for synthesis of other polymers and macromolecules in biological processes having either a defined sequence of nucleotides (for example, rRNA, tRNA and mRNA) or a defined sequence of amino acids and the biological properties resulting therefrom. Thus, a gene encodes a protein if transcription and translation of mRNA produced by that gene produces the protein in a cell or other biological system. Both the coding strand, the nucleotide sequence of which is identical to the mRNA sequence and is usually provided in sequence listings, and non-coding strand, used as the template for transcription, of a gene or cDNA can be referred to as encoding the protein or other product of that gene or cDNA. Unless otherwise specified, a “nucleotide sequence encoding an amino acid sequence” includes all nucleotide sequences that are degenerate versions of each other and that encode the same amino acid sequence. Nucleotide sequences that encode proteins and RNA may include introns.

“Recombinant nucleic acid” refers to a nucleic acid having nucleotide sequences that are not naturally joined together. This includes nucleic acid vectors comprising an amplified or assembled nucleic acid which can be used to transform a suitable host cell. A host cell that comprises the recombinant nucleic acid is referred to as a “recombinant host cell.” The gene is then expressed in the recombinant host cell to produce, such as a “recombinant polypeptide.” A recombinant nucleic acid may serve a non-coding function (such as a promoter, origin of replication, ribosome-binding site, etc.) as well.

A first sequence is an “antisense” with respect to a second sequence if a polynucleotide whose sequence is the first sequence specifically hybridizes with a polynucleotide whose sequence is the second sequence.

Terms used to describe sequence relationships between two or more nucleotide sequences or amino acid sequences include “reference sequence,” “selected from,” “comparison window,” “identical,” “percentage of sequence identity,” “substantially identical,” “complementary,” and “substantially complementary.”

For sequence comparison of nucleic acid sequences and amino acids sequences, typically one sequence acts as a reference sequence, to which test sequences are compared. When using a sequence comparison algorithm, test and reference sequences are entered into a computer, subsequence coordinates are designated, if necessary, and sequence algorithm program parameters are designated. Default program parameters are used. Methods of alignment of sequences for comparison are well known in the art. Optimal alignment of sequences for comparison can be conducted, for example, by the local homology algorithm of Smith & Waterman, Adv. Appl. Math. 2:482, 1981, by the homology alignment algorithm of Needleman & Wunsch, J. Mol. Biol. 48:443, 1970, by the search for similarity method of Pearson & Lipman, Proc. Nat'l. Acad. Sci. USA 85:2444, 1988, by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, Wis.), or by manual alignment and visual inspection (see for example, Current Protocols in Molecular Biology (Ausubel et al, eds 1995 supplement)).

One example of a useful algorithm is PILEUP. PILEUP uses a simplification of the progressive alignment method of Feng & Doolittle, J. Mol. Evol. 35:351-360, 1987. The method used is similar to the method described by Higgins & Sharp, CABIOS 5:151-153, 1989. Using PILEUP, a reference sequence is compared to other test sequences to determine the percent sequence identity relationship using the following parameters: default gap weight (3.00), default gap length weight (0.10), and weighted end gaps. PILEUP can be obtained from the GCG sequence analysis software package, such as version 7.0 (Devereaux et al., Nuc. Acids Res. 12:387-395, 1984.

Another example of algorithms that are suitable for determining percent sequence identity and sequence similarity are the BLAST and the BLAST 2.0 algorithm, which are described in Altschul et al., J. Mol. Biol. 215:403-410, 1990 and Altschul et al., Nucleic Acids Res. 25:3389-3402, 1977. Software for performing BLAST analyses is publicly available through the National Center for Biotechnology Information (http://www.ncbi.nlm.nih.gov/). The BLASTN program (for nucleotide sequences) uses as defaults a word length (W) of 11, alignments (B) of 50, expectation (E) of 10, M=5, N=−4, and a comparison of both strands. The BLASTP program (for amino acid sequences) uses as defaults a word length (W) of 3, and expectation (E) of 10, and the BLOSUM62 scoring matrix (see Henikoff & Henikoff, Proc. Natl. Acad. Sci. USA 89:10915, 1989).

Another indicia of sequence similarity between two nucleic acids is the ability to hybridize. The more similar are the sequences of the two nucleic acids, the more stringent the conditions at which they will hybridize. The stringency of hybridization conditions are sequence-dependent and are different under different environmental parameters. Thus, hybridization conditions resulting in particular degrees of stringency will vary depending upon the nature of the hybridization method of choice and the composition and length of the hybridizing nucleic acid sequences. Generally, the temperature of hybridization and the ionic strength (especially the Na⁺ and/or Mg⁺⁺ concentration) of the hybridization buffer will determine the stringency of hybridization, though wash times also influence stringency. Generally, stringent conditions are selected to be about 5° C. to 20° C. lower than the thermal melting point (T_(m)) for the specific sequence at a defined ionic strength and pH. The T_(m) is the temperature (under defined ionic strength and pH) at which 50% of the target sequence hybridizes to a perfectly matched probe. Conditions for nucleic acid hybridization and calculation of stringencies can be found, for example, in Sambrook et al., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 2001; Tijssen, Hybridization With Nucleic Acid Probes, Part I: Theory and Nucleic Acid Preparation, Laboratory Techniques in Biochemistry and Molecular Biology, Elsevier Science Ltd., NY, N.Y., 1993. and Ausubel et al. Short Protocols in Molecular Biology, 4^(th) ed., John Wiley & Sons, Inc., 1999.

“Stringent conditions” encompass conditions under which hybridization will only occur if there is less than 25% mismatch between the hybridization molecule and the target sequence. “Stringent conditions” may be broken down into particular levels of stringency for more precise definition. Thus, as used herein, “moderate stringency” conditions are those under which molecules with more than 25% sequence mismatch will not hybridize; conditions of “medium strigency” are those under which molecules with more than 15% mismatch will not hybridize, and conditions of “high stringency” are those under which sequences with more than 10% mismatch will not hybridize. Conditions of “very high stringency” are those under which sequences with more than 6% mismatch will not hybridize. In contrast nucleic acids that hybridize under “low stringency conditions include those with much less sequence identity, or with sequence identity over only short subsequences of the nucleic acid. For example, a nucleic acid construct can include a polynucleotide sequence that hybridizes under high stringency or very high stringency, or even higher stringency conditions to a polynucleotide sequence that encodes SEQ ID NO: 1.

Operably linked: A first nucleic acid sequence is operably linked with a second nucleic acid sequence when the first nucleic acid sequence is placed in a functional relationship with the second nucleic acid sequence. For instance, a promoter is operably linked to a coding sequence if the promoter affects the transcription or expression of the coding sequence. Generally, operably linked DNA sequences are contiguous and, where necessary to join two protein-coding regions, in the same reading frame.

Peptide Modifications: The present disclosure includes mutant gp120 peptides, as well as synthetic embodiments. In addition, analogues (non-peptide organic molecules), derivatives (chemically functionalized peptide molecules obtained starting with the disclosed peptide sequences) and variants (homologs) of gp120 can be utilized in the methods described herein. The peptides disclosed herein include a sequence of amino acids that can be either L- and/or D-amino acids, naturally occurring and otherwise.

Peptides can be modified by a variety of chemical techniques to produce derivatives having essentially the same activity as the unmodified peptides, and optionally having other desirable properties. For example, carboxylic acid groups of the protein, whether carboxyl-terminal or side chain, may be provided in the form of a salt of a pharmaceutically-acceptable cation or esterified to form a C₁-C₁₆ ester, or converted to an amide of formula NR₁R₂ wherein R₁ and R₂ are each independently H or C₁-C₁₆ alkyl, or combined to form a heterocyclic ring, such as a 5- or 6-membered ring. Amino groups of the peptide, whether amino-terminal or side chain, may be in the form of a pharmaceutically-acceptable acid addition salt, such as the HCl, HBr, acetic, benzoic, toluene sulfonic, maleic, tartaric and other organic salts, or may be modified to C₁-C₁₆ alkyl or dialkyl amino or further converted to an amide.

Hydroxyl groups of the peptide side chains can be converted to C₁-C₁₆ alkoxy or to a C₁-C₁₆ ester using well-recognized techniques. Phenyl and phenolic rings of the peptide side chains can be substituted with one or more halogen atoms, such as F, Cl, Br or I, or with C₁-C₁₆ alkyl, C₁-C₁₆ alkoxy, carboxylic acids and esters thereof, or amides of such carboxylic acids. Methylene groups of the peptide side chains can be extended to homologous C₂-C₄ alkylenes. Thiols can be protected with any one of a number of well-recognized protecting groups, such as acetamide groups. Those skilled in the art will also recognize methods for introducing cyclic structures into the peptides of this disclosure to select and provide conformational constraints to the structure that result in enhanced stability. For example, a C- or N-terminal cysteine can be added to the peptide, so that when oxidized the peptide will contain a disulfide bond, generating a cyclic peptide. Other peptide cyclizing methods include the formation of thioethers and carboxyl- and amino-terminal amides and esters.

Peptidomimetic and organomimetic embodiments are also within the scope of the present disclosure, whereby the three-dimensional arrangement of the chemical constituents of such peptido- and organomimetics mimic the three-dimensional arrangement of the peptide backbone and component amino acid side chains, resulting in such peptido- and organomimetics of the proteins of this disclosure. For computer modeling applications, a pharmacophore is an idealized, three-dimensional definition of the structural requirements for biological activity. Peptido- and organomimetics can be designed to fit each pharmacophore with current computer modeling software (using computer assisted drug design or CADD). See Walters, “Computer-Assisted Modeling of Drugs”, in Klegerman & Groves, eds., 1993, Pharmaceutical Biotechnology, Interpharm Press: Buffalo Grove, Ill., pp. 165-174 and Principles of Pharmacology Munson (ed.) 1995, Ch. 102, for descriptions of techniques used in CADD. Also included within the scope of the disclosure are mimetics prepared using such techniques. In one example, a mimetic minics the antigenic activity generated by gp120 a mutant, a variant, fragment, or fusion thereof.

Pharmaceutical agent: A chemical compound or composition capable of inducing a desired therapeutic or prophylactic effect when properly administered to a subject or a cell. “Incubating” includes a sufficient amount of time for a drug to interact with a cell. “Contacting” includes incubating a drug in solid or in liquid form with a cell. An “anti-viral agent” or “anti-viral drug” is an agent that specifically inhibits a virus from replicating or infecting cells. Similarly, an “anti-retroviral agent” is an agent that specifically inhibits a retrovirus from replicating or infecting cells.

A “therapeutically effective amount” is a quantity of a chemical composition or an anti-viral agent sufficient to achieve a desired effect in a subject being treated. For instance, this can be the amount necessary to inhibit viral replication or to measurably alter outward symptoms of the viral infection, such as increase of T cell counts in the case of an HIV-I infection. In general, this amount will be sufficient to measurably inhibit virus (for example, HIV) replication or infectivity. When administered to a subject, a dosage will generally be used that will achieve target tissue concentrations (for example, in lymphocytes) that has been shown to achieve in vitro inhibition of viral replication.

Pharmaceutically acceptable carriers: The pharmaceutically acceptable carriers of use are conventional. Remington's Pharmaceutical Sciences, by E. W. Martin, Mack Publishing Co., Easton, Pa., 15th Edition, 1975, describes compositions and formulations suitable for pharmaceutical delivery of the fusion proteins herein disclosed.

In general, the nature of the carrier will depend on the particular mode of administration being employed. For instance, parenteral formulations usually comprise injectable fluids that include pharmaceutically and physiologically acceptable fluids such as water, physiological saline, balanced salt solutions, aqueous dextrose, glycerol or the like as a vehicle. For solid compositions (such as powder, pill, tablet, or capsule forms), conventional non-toxic solid carriers can include, for example, pharmaceutical grades of mannitol, lactose, starch, or magnesium stearate. In addition to biologically neutral carriers, pharmaceutical compositions to be administered can contain minor amounts of non-toxic auxiliary substances, such as wetting or emulsifying agents, preservatives, and pH buffering agents and the like, for example sodium acetate or sorbitan monolaurate.

Polypeptide: Any chain of amino acids, regardless of length or post-translational modification (such as glycosylation or phosphorylation). “Polypeptide” applies to amino acid polymers to naturally occurring amino acid polymers and non-naturally occurring amino acid polymer as well as in which one or more amino acid residue is a non-natural amino acid, for example a artificial chemical mimetic of a corresponding naturally occurring amino acid. In one embodiment, the polypeptide is a gp120 polypeptide, such as a stabilized gp120. A “residue” refers to an amino acid or amino acid mimetic incorporated in a polypeptide by an amide bond or amide bond mimetic. A polypeptide has an amino terminal (N-terminal) end and a carboxy terminal (C-terminal) end. “Polypeptide” is used interchangeably with peptide or protein, and is used interchangeably herein to refer to a polymer of amino acid residues.

Protein core: The protein core refers to the interior of a folded protein, which is substantially free of solvent exposure, such as solvent in the form of water molecules in solution. Typically, the protein core is predominately composed of hydrophobic or apolar amino acids. In some examples, a protein core may contain charged amino acids, for example aspartic acid, glutamic acid, arginine, and/or lysine. The inclusion of uncompensated charged amino acids (a compensated charged amino can be in the form of a salt bridge) in the protein core can lead to a destabilized protein. That is, a protein with a lower T_(m) then a similar protein without an uncompensated charged amino acid in the protein core. In other examples, a protein core may have a cavity with in the protein core. Cavities are essentially voids within a folded protein where amino acids or amino acid side chains are not present. Such cavities can also destabilize a protein relative to a similar protein without a cavity. Thus, when creating a stabilized form of a protein, for example a stabilized form of gp120, it may be advantageous to substitute amino acid residues within the core in order to fill cavities present in the wild-type protein.

Purified: The term purified does not require absolute purity; rather, it is intended as a relative term. Thus, for example, a purified protein is one in which the protein is more enriched than the protein is in its natural environment within a cell. Preferably, a preparation is purified such that the protein represents at least 50% of the protein content of the preparation.

The gp120 polypeptides disclosed herein, or antibodies that specifically bind gp120, can be purified by any of the means known in the art. See for example Guide to Protein Purification, ed. Deutscher, Meth. Enzymol. 185, Academic Press, San Diego, 1990; and Scopes, Protein Purification: Principles and Practice, Springer Verlag, New York, 1982. Substantial purification denotes purification from other proteins or cellular components. A substantially purified protein is at least 60%, 70%, 80%, 90%, 95% or 98% pure. Thus, in one specific, non-limiting example, a substantially purified protein is 90% free of other proteins or cellular components.

Space Group: The arrangement of symmetry elements of a crystal.

Structure coordinates: Mathematical coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) such as a gp120, a gp120:CD4 complex, a gp120:antibody complex, or combinations thereof in a crystal in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal. In one example, the term “structure coordinates” refers to Cartesian coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays, such as by the atoms of a stabilized form of gp120 in crystal form.

Atomic coordinate data, such as that in Table 1 lists each atom by a unique number (column 2); the atom name in the context of the residue to which it belongs (column 3), for example CA refers to the alpha carbon of the peptide backbone (detailed descriptions of the atom identifiers for each residue can be found for example in Creighton, Proteins, Structures and Molecular Properties, W.H. Freeman & Co., New York, 1993); the amino acid residue in which the atom is located (column 4); the chain identifier (column 4′) which may or may not be included, the number of the residue (column 5); the coordinates (for example, X, Y, Z) which define with respect to the crystallographic axes the atomic position (in A) of the respective atom (columns 6, 7, and 8); the occupancy of the atom in the respective position (column 9); the “B-factor”, which is the isotropic displacement parameter (in Å²) and accounts for movement of the atom around its atomic center (column 10).

Those of ordinary skill in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. For the purpose of this disclosure, any set of structure coordinates for a stabilized form of gp120 or a gp120 with an extended V3 loop that have a root mean square deviation of protein backbone atoms (N, Cα, C and 0) of less than about 1.0 Angstroms when superimposed, such as about 0.75, or about 0.5, or about 0.25 Angstroms, using backbone atoms, on the structure coordinates listed in Table 1 shall (in the absence of an explicit statement to the contrary) be considered identical.

Subject: Living multi-cellular vertebrate organisms, a category that includes both human and veterinary subjects, including human and non-human mammals.

T Cell: A white blood cell critical to the immune response. T cells include, but are not limited to, CD4⁺ T cells and CD8⁺ T cells. A CD4⁺ T lymphocyte is an immune cell that carries a marker on its surface known as “cluster of differentiation 4” (CD4). These cells, also known as helper T cells, help orchestrate the immune response, including antibody responses as well as killer T cell responses. CD8⁺ T cells carry the “cluster of differentiation 8” (CD8) marker. In one embodiment, a CD8 T cells is a cytotoxic T lymphocytes. In another embodiment, a CD8 cell is a suppressor T cell.

Therapeutic agent: Used in a generic sense, it includes treating agents, prophylactic agents, and replacement agents.

T_(m): The temperature at which a change of state occurs. For example, the temperature at which gp120 undergoes a transition from the folded form to the unfolded form. Essentially this is the temperature at which the structure melts away. Stabilized gp120 has a higher T_(m) than native gp120. Another example would be the temperature at which a DNA duplex melts.

Transformed: A transformed cell is a cell into which has been introduced a nucleic acid molecule by molecular biology techniques. As used herein, the term transformation encompasses all techniques by which a nucleic acid molecule might be introduced into such a cell, including transfection with viral vectors, transformation with plasmid vectors, and introduction of DNA by electroporation, lipofection, and particle gun acceleration.

Unit Cell: The smallest building block of a crystal. The entire volume of a crystal may be constructed by regular assembly of such blocks. Each unit cell comprises a complete representation of the unit of pattern, the repetition of which builds produces a crystal lattice

Vector: A nucleic acid molecule as introduced into a host cell, thereby producing a transformed host cell. Recombinant DNA vectors are vectors having recombinant DNA. A vector can include nucleic acid sequences that permit it to replicate in a host cell, such as an origin of replication. A vector can also include one or more selectable marker genes and other genetic elements known in the art. Viral vectors are recombinant DNA vectors having at least some nucleic acid sequences derived from one or more viruses.

Virus: Microscopic infectious organism that reproduces inside living cells. A virus consists essentially of a core of a single nucleic acid surrounded by a protein coat, and has the ability to replicate only inside a living cell. “Viral replication” is the production of additional virus by the occurrence of at least one viral life cycle. A virus may subvert the host cells' normal functions, causing the cell to behave in a manner determined by the virus. For example, a viral infection may result in a cell producing a cytokine, or responding to a cytokine, when the uninfected cell does not normally do so.

“Retroviruses” are RNA viruses wherein the viral genome is RNA. When a host cell is infected with a retrovirus, the genomic RNA is reverse transcribed into a DNA intermediate which is integrated very efficiently into the chromosomal DNA of infected cells. The integrated DNA intermediate is referred to as a provirus. The term “lentivirus” is used in its conventional sense to describe a genus of viruses containing reverse transcriptase. The lentiviruses include the “immunodeficiency viruses” which include human immunodeficiency virus (HIV) type 1 and type 2 (HIV-I and HIV-II), simian immunodeficiency virus (SIV), and feline immunodeficiency virus (FIV).

HIV-I is a retrovirus that causes immunosuppression in humans (HIV disease), and leads to a disease complex known as the acquired immunodeficiency syndrome (AIDS). “HIV disease” refers to a well-recognized constellation of signs and symptoms (including the development of opportunistic infections) in persons who are infected by an HIV virus, as determined by antibody or western blot studies. Laboratory findings associated with this disease are a progressive decline in T cells.

ΔS: The change in entropy, such as the change in entropy upon the association of gp120 and CD4 or an antibody or antibody fragment, for example X5.

ΔH: The change in enthalpy, such as the change in enthalpy upon the association of gp120 and b12 or CD4.

II. Overview of Several Embodiments

Provided herein in various embodiments are gp120 polypeptides, which are useful to induce immunogenic response in vertebrate animals (such as mammals, for example primates, such as humans) to lentivirus, such as SIV or HIV (for example HIV-I and HIV-II).

In several embodiments, the gp120 polypeptides are stabilized in a CD4 bound conformation. In several disclosed examples, the gp120 polypeptides are stabilized by modification. In certain examples, these modifications can be the introduction of a plurality of non-naturally occurring cross-linking cysteine residues. In certain examples, the modification can be the introduction of at least one amino acid substitution in the core of gp120.

In one example, cysteines are introduced into the gp120 polypeptide at position 96, 109, 123, 231, 267, 275, 428, 431, or in combinations thereof. In some examples of gp120 polypeptides disclosed herein, the plurality of non-naturally occurring cross-linking cysteine residues are defined by the interaction and crosslinking of at least one of residue pairs 96 and 275; 109 and 428; 123 and 431; and 231 and 267. In one embodiment, the residue pairs 96 and 275 and 109 and 428 are crosslinked.

In some embodiments, the stabilized gp120 polypeptide contains one or more amino acid substitutions in the protein core. In several examples, the substitution is made at position 95, 257, 375, 433, or a combination thereof. In specific examples, the substitution is a serine to tryptophan substitution at position 95, a threonine to serine substitution at position 257, a serine to tryptophan substitution at position 375, an alanine to methionine substitution at position 433, or a combination thereof.

In a specific example, the stabilized gp120 polypeptide includes the amino acid sequence set forth as SEQ ID NO: 1. In still other embodiments, the stabilized gp120 contains a portion of the amino acid sequence set forth as SED ID NO: 1, for example, a domain such as the outer domain, or a contiguous stretch of about 5 or more amino acids, such as about 6, about 7, about 8, about 9, about 10, about 15, about 20, about 25, or more amino acids.

Other embodiments are compositions containing a therapeutically effective amount of at least one gp120 polypeptide, such as a stabilized gp120 polypeptide (such as set forth as SEQ ID NO: 1). In some embodiments, the composition can contain pharmaceutically acceptable carriers, adjuvants, or combinations thereof.

This disclosure further provides methods for eliciting and/or enhancing an immune response in a subject (such as a primate subject, for example a human subject). In some embodiments, these methods involve administering to the subject a composition including a gp120 polypeptide as disclosed herein, for example a stabilized gp120 such as set forth as SEQ ID NO: 1. In one specific, non-limiting example, the subject is infected with a lentivirus, for example SIV or HIV, such as HIV-I or HIV-II. In some embodiments, the immune response is a B cell response, a T cell response, or a combination thereof.

In other embodiments, the subject is further administered a therapeutically effective amount of a monomeric or trimeric gp140 polypeptide, a monomeric or trimeric gp120 polypeptide, or a combination thereof.

Other embodiments of this disclosure are isolated polynucleotides (nucleic acid molecules) which encode the gp120 polypeptides described herein. Specific examples of such nucleic acid molecules contain nucleic acids encoding the amino acid sequence set forth as SEQ ID NO: 1 or degenerate variants thereof. In other embodiments, the isolated polynucleotides consist of nucleic acid molecules encoding the amino acid sequence set forth as one of SEQ ID NO: 1 or degenerate variants thereof. In certain embodiments, the nucleic acid molecule encoding a gp120 polypeptide is operably linked to a promoter. Vectors comprising such polynucleotides are also disclosed, as are host cells transformed with such vectors.

Other embodiments are compositions containing a therapeutically effective amount of a polynucleotide containing a nucleic acid molecule encoding a gp120 polypeptide disclosed herein. In certain embodiments, the nucleic acid molecule encodes the amino acid sequence set forth as SEQ ID NO: 1. In some embodiments the composition can contain pharmaceutically acceptable carriers, adjuvants, or combinations thereof.

This disclosure further provides methods for eliciting and/or enhancing an immune response in a subject (such as a primate subject, for example a human subject). The methods involve administering to the subject a composition containing a nucleic acid molecule encoding a gp120 polypeptide of this disclosure. In one specific, non-limiting example, the subject is infected with a lentivirus, for example SIV or HIV, such as HIV-I or HIV-II. In some embodiments the immune response is a B cell response, a T cell response, or a combination thereof.

In other embodiments, the subject is further administered a therapeutically effective amount of a plasmid vector expressing a polypeptide containing a monomeric or trimeric gp140 polypeptide, an monomeric or trimeric gp120 polypeptide; or combination thereof.

Also disclosed herein are methods for identifying an immunogen that induces an immune response to gp120, for example gp120 from a lentivirus, such as SIV or HIV such as HIV-I or HIV-II. Typically the immune response is a B cell response, a T cell response, or a combination thereof. These methods involve using a three-dimensional structure of gp120 as defined by atomic coordinates set forth in Table 1 or a subset of the coordinates of Table 1 to design or select the immunogen, synthesizing the immunogen, immunizing a subject with the immunogen; and determining if an immune response to gp120 is induced in the subject. In some embodiments, the immunogen is designed from the gp120 amino acid sequence. In certain embodiments, the immunogen is designed or selected using a three-dimensional structure of gp120 as defined by atomic coordinates set forth in Table 1 or a subset of the coordinates of Table 1 and an amino acid sequence is assembled to provide an immunogen, for example by synthesizing the amino acid sequence or producing a nucleic acid molecule encoding the immunogen.

Also provided by this disclosure is a machine readable data storage medium including a data storage material encoded with machine readable data corresponding to the coordinates of a stabilized form of gp120 as defined by Table 1 or a subset of the coordinates of Table I.

Also provided for are computer systems including data and a data processor, wherein the system forms a representation of the three-dimensional structure gp120 protein as defined by the coordinates set forth in Table 1 or a subset of the coordinates of Table 1, such as the atomic positions, surface, domain, or region of the gp120 polypeptide.

Also disclosed herein is the use of stabilized gp120 molecules as crystallization tools. A crystalline form of a stabilized gp120 also is disclosed, for example the crystalline form of gp120 as defined by the coordinates as given in Table 1, or with coordinates having a root mean square deviation therefrom, wherein the distance between the residues is less than about 0.75 Å.

III. gp120 Immunogens and Nucleic Acids Encoding gp120 Immunogens

The present disclosure relates to gp120 polypeptides and nucleic acids encoding these gp120 polypeptides. The gp120 polypeptides of this disclosure are capable of eliciting an immune response to a gp120 protein in a subject, such as a human subject. In some embodiments, the gp120 polypeptides of this disclosure are stabilized in a CD4 bound conformation.

Using a combination of atomic level structural information with biophysical techniques gp120 polypeptides were designed that are stabilized in the conformation substantially identical to the CD4 bound polypeptide. For example, the three-dimensional structure of the wild-type polypeptide was analyzed to determine where cysteine residues could be introduced such that they would form disulfide bonds in the folded molecule. This methodology is not specific to cysteine residues; other natural or non-natural amino acids could be used. In some embodiments, the stabilized gp120 has a K_(d) for CD4 of less than or equal to about 10 nM, such as less than or equal to about 5 nM, less than or equal to about 3 nM, or less than or equal to about 1 nM. In some embodiments the stabilized gp120 has −TΔS for CD4 binding of about less than or equal to 40 kcal/mol, such as about less than or equal to 30 kcal/mol, about less than or equal to 15 kcal/mol, or about less than or equal to 10 kcal/mol.

The stability of folded polypeptides can be measured using techniques such as thermal denaturation. The temperature of the unfolding transition (T_(m)) is an accepted measure of the stability of the folded polypeptide, where increases in T_(m) indicate an increase in the stability of the folded polypeptide. In some embodiments, the stabilized gp120 polypeptides has a T_(m) value greater than about 52° C., such as greater than about 53° C., greater than about 54° C. (such as 53.8° C.), greater than about 55° C., greater than about 56° C., greater than about 57° C., greater than about 58° C., or even grater than about 59° C.

In some embodiments, the stabilized gp120 polypeptides are stabilized by a plurality of non-naturally occurring cross-linking cysteine residues. By plurality it is meant that there are at least 2, such as at least 4, at least 6, or at least 8 cysteines introduced by mutation into a gp120 polypeptide, such that pairs of cysteines form at least 1, such as at least 2, at least 3, or at least 4 disulfide bonds. Each disulfide bond is formed by a pair of cysteines.

In some embodiments, the mutationally introduced cysteines are introduced into the gp120 polypeptide at positions 96, 109, 123, 231, 267, 275, 428, 431, or in a sub-combination thereof. In some examples of the stabilized gp120 polypeptides, the plurality of non-naturally occurring cross-linking cysteine residues are defined by the interaction of at least one of residue pairs 96 and 275; 109 and 428; 123 and 431; and 231 and 267. Thus, the stabilized gp120 polypeptides of this disclosure may have any combination of the crosslinked cysteines defined by the interaction of 96 and 275; 109 and 428; 123 and 431; and 231 and 267.

In some embodiments, the stabilized gp120 polypeptide contains one or more amino acid substitutions in the protein core. In several disclosed examples, the substitution is made at position 95, 257, 375, 433, or a combination thereof. Thus, a stabilized gp120 polypeptide may have one, two, three, or four substitutions in the protein core. In specific examples, the substitution is a serine to tryptophan substitution at position 95, a threonine to serine substitution at position 257, a serine to tryptophan substitution at position 375, an alanine to methionine substitution at position 433, or various combinations thereof.

In one embodiment, the stabilized gp120 polypeptide is stabilized in a CD4 binding conformation by crosslinked cysteines defined by the interaction of 96 and 275; 109 and 428; and amino acid substitutions in the protein core, wherein the substitutions are a serine to tryptophan substitution at position 95, a threonine to serine substitution at position 257, a serine to tryptophan substitution at position 375, an alanine to methionine substitution at position 433.

In one example, the stabilized gp120 polypeptide includes the amino acid sequence set forth as:

(SEQ ID NO: 1) EVVLVNVTEN FNWCKNDMVE QMHEDICSLW DQSLKPCVKL TPLCVGAGSC NTSVITQACP KVSFEPIPIH YCAPAGFAIL KCNNKTFNGT GPCTNVSTVQ CTHGIRPVVS SQLLLNGSLA EEEVVIRSVC FTDNAKTIIV QLNTSVEINC TGAGHCNISR AKWNNTLKQI ASKLREQFGN NKTIIFKQSS GGDPEIVTHW FNCGGEFFYC NSTQLFNSTW FNSTWSTKGS NNTEGSDTIT LPCRIKQIIN MWCKVGKMMY APPISGQIRC SSNITGLLLT RDGGNSNNES EIFRPGGGDM RDNWRSELYK YKVVKIE.

Thus, a stabilized gp120 polypeptide can contain the amino acid sequence set forth as SEQ ID NO: 1 or a fragment thereof. In one example the stabilized gp120 polypeptide consists of the amino acid sequence set forth as SEQ ID NO: 1 or a fragment thereof. The present disclosure provides stabilized gp120 fragments that are suitable for use in inducing an immune response in a subject. In some embodiments, a stabilized gp120 polypeptide is an immunogenic fragment of SEQ ID NO: 1, such that the immunogenic fragment is stabilized in a CD4 binding conformation by crosslinked cysteines defined by the interaction of 96 and 275; 109 and 428; and amino acid substitutions in the protein core, wherein the substitutions are a serine to tryptophan substitution at position 95, a threonine to serine substitution at position 257, a serine to tryptophan substitution at position 375, an alanine to methionine substitution at position 433. In some embodiments, the stabilized gp120 includes the outer-domain. In one example, the outer domain includes residues 255-421 and 436-474 of gp120. Thus, the outer domain can contain residues 109-246 and 261-299 of SEQ ID NO: 1. In some examples residues 246 and 261 are covalently linked, for example by a peptide linker. In some examples, the peptide linker is residues 247-260 of SEQ ID NO: 1. Ideally the linker should be of sufficient length such that the folded protein is a conformation that can be bound by CD4. In some embodiments, the linker is a peptide linker and the peptide linker is about 2 to about 20 amino acids in length, such as about 2, about 3, about 4, about 5, about 6, about 7, about 8, about 10, about 12, about 15, or about 20 amino acids in length. In some embodiments, the immunogenic fragment of gp120 consists of residues 109-246 and 261-299, and a linker. In some embodiments the linker does not contain a sequence from gp120.

In other embodiments, the stabilized gp120 fragment is truncated on the carboxy terminal end. For example the carboxy terminal end can be truncated to about amino acid residue 433. In addition, portions of the amino terminus of gp120 can also be eliminated from the stabilized gp120 fragment. The truncated gp120 sequence can be free from the carboxy terminus through amino acid residue 95. In one embodiment, the truncated gp120 sequence is free from the amino terminus of gp120 through residue 95 and residue 433 through the carboxy terminus of gp120. In other embodiments, the gp120 polypeptide has an amino acid sequence least 90% identical to SEQ ID NO: 1, for example a polypeptide that has about 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or even higher sequence identity to SEQ ID NO: 1.

The immunogenic gp120 polypeptides, or immunogenic fragments of the gp120 polypeptides disclosed herein can be chemically synthesized by standard methods, or can be produced recombinantly. An exemplary process for polypeptide production is described in Lu et al., Federation of European Biochemical Societies Letters. 429:31-35, 1998. They can also be isolated by methods including preparative chromatography and immunological separations.

In other embodiments, fusion proteins are provided including a first and second polypeptide moiety in which one of the protein moieties includes an amino acid sequence as set forth in SEQ ID NO: 1 or a fragment thereof. The other moiety is a heterologous protein such as can be a carrier protein and/or an immunogenic protein. Such fusions also are useful to evoke an immune response against gp120. In certain embodiments the gp120 polypeptides disclosed herein are co-valent or non-covalent addition of toll like receptor (TLR) ligands or dendritic cell or B cell targeting moieties.

A gp120 polypeptide can be covalently linked to a carrier, which is an immunogenic macromolecule to which an antigenic molecule can be bound. When bound to a carrier, the bound polypeptide becomes more immunogenic. Carriers are chosen to increase the immunogenicity of the bound molecule and/or to elicit higher titers of antibodies against the carrier which are diagnostically, analytically, and/or therapeutically beneficial. Covalent linking of a molecule to a carrier can confer enhanced immunogenicity and T cell dependence (see Pozsgay et al., PNAS 96:5194-97, 1999; Lee et al., J. Immunol. 116:1711-18, 1976; Dintzis et al., PNAS 73:3671-75, 1976). Useful carriers include polymeric carriers, which can be natural (for example, polysaccharides, polypeptides or proteins from bacteria or viruses), semi-synthetic or synthetic materials containing one or more functional groups to which a reactant moiety can be attached. Bacterial products and viral proteins (such as hepatitis B surface antigen and core antigen) can also be used as carriers, as well as proteins from higher organisms such as keyhole limpet hemocyanin, horseshoe crab hemocyanin, edestin, mammalian serum albumins, and mammalian immunoglobulins. Additional bacterial products for use as carriers include bacterial wall proteins and other products (for example, streptococcal or staphylococcal cell walls and lipopolysaccharide (LPS)).

Most antigenic epitopes of HIV proteins are relatively small in size, such as about 5 to 100 amino acids in size, for example about 5, about 6, about 7, about 8, about 9, about 10, about 15, about 20, about 25, about 30, about 40, about 50, about 60, about 70, about 80, about 90, or about 100. Thus, fragments (for example, epitopes or other antigenic fragments) of a gp120 polypeptide, such as any of the gp120 polypeptides described herein or a fragment thereof, can be used as an immunogen. In certain embodiments, the antigenic fragment of gp120 includes the outerdomain of gp120. In some embodiment, the stabilized gp120 includes the outer-domain. In one example, the outer domain includes residues 255-421 and 436-474 of gp120. Thus, the outer domain can include residues 109-246 and 261-299 of SEQ ID NO: 1.

In some embodiments, the disclosed gp120 polypeptides are modified by glycosylation, for example by N-linked glycans. Thus, the immune response can be focused on a region interest of a gp120 polypeptide by masking other regions with non-immunogenic glycans. Glycosylation sites can be introduced into the gp120 polypeptides by site directed mutagenesis. This straggly can be utilized to focus the immune response to regions of interest in the gp120 polypeptide, for example the CD4 binding site or the binding site for a neutralizing antibody, for example a the b12 antibody. Examples of glycan masking can be found in Pantophlet and Burton, Trends Mol. Med. 9(11):468-73, 2003, which is incorporated by reference herein in its entirety.

Another strategy to focus the immune response on the CD4 binding region or b12 epitope region is to use SIV and HIVgp120 core glycoproteins (such as the stabilized gp120 polypeptides disclosed herein) that possess an endogenous CD4 binding site or to scaffold the heterologous HIV-1 CD4 binding region onto cores derived from selected SIV or HIV-2 strains. The gp120 core can be derived from the envelope glycoproteins of letivius, for example SIV such as SIV mac239 and HIV, such as HIV-2 7132A. The residues required for CD4BS antibody recognition, for example the site of b12 binding, are transplanted by site-directed mutagenesis of the appropriate codon-optimized plasmid sequences. In some embodiments, N-glycans are added to these cores to eliminate the elicitation of non-cross reactive antibodies directed against regions outside the antibody binding site, for example the binding site of a neutralizing antibody such as CD4BS antibody.

The present disclosure concerns nucleic acid constructs including polynucleotide sequences that encode antigenic gp120 polypeptides of HIV-I. These polynucleotides include DNA, cDNA and RNA sequences which encode the polypeptide of interest.

Methods for the manipulation and insertion of the nucleic acids of this disclosure into vectors are well known in the (see for example, Sambrook et al., Molecular Cloning, a Laboratory Manual, 2d edition, Cold Spring Harbor Press, Cold Spring Harbor, N.Y., 1989, and Ausubel et al., Current Protocols in Molecular Biology, Greene Publishing Associates and John Wiley & Sons, New York, N.Y., 1994).

Typically, the nucleic acid constructs encoding the gp120 polypeptides of this disclosure are plasmids. However, other vectors (for example, viral vectors, phage, cosmids, etc.) can be utilized to replicate the nucleic acids. In the context of this disclosure, the nucleic acid constructs typically are expression vectors that contain a promoter sequence which facilitates the efficient transcription of the inserted genetic sequence of the host. The expression vector typically contains an origin of replication, a promoter, as well as specific nucleic acid sequences that allow phenotypic selection of the transformed cells.

More generally, polynucleotide sequences encoding the gp120 polypeptides of this disclosure can be operably linked to any promoter and/or enhancer that is capable of driving expression of the nucleic acid following introduction into a host cell. A promoter is an array of nucleic acid control sequences that directs transcription of a nucleic acid. A promoter includes necessary nucleic acid sequences (which can be) near the start site of transcription, such as in the case of a polymerase II type promoter (a TATA element). A promoter also can include distal enhancer or repressor elements which can be located as much as several thousand base pairs from the start site of transcription. Both constitutive and inducible promoters are included (see, for example, Bitter et al., Methods in Enzymology 153:516-544, 1987).

To produce such nucleic acid constructs, polynucleotide sequences encoding gp120 polypeptides are inserted into a suitable expression vector, such as a plasmid expression vector. Procedures for producing polynucleotide sequences encoding gp120 polypeptides and for manipulating them in vitro are well known to those of skill in the art, and can be found, for example in Sambrook and Ausubel, supra.

In addition to the polynucleotide sequences encoding the polypeptides set forth as SEQ ID NO: 1 disclosed herein, the nucleic acid constructs can include variant polynucleotide sequences that encode polypeptides that are substantially similar to SEQ ID NO: 1. Similarly, the nucleic acid constructs can include polynucleotides that encode chimeric polypeptides, for example fusion proteins. For enhanced immunogenicity, a sequence encoding for heterologous T helper sequence derived from HIV or other heterologous source can be included in the molecule.

The similarity between amino acid (and polynucleotide) sequences is expressed in terms of the similarity between the sequences, otherwise referred to as sequence identity. Sequence identity is frequently measured in terms of percentage identity (or similarity); the higher the percentage, the more similar are the primary structures of the two sequences. In general, the more similar the primary structures of two amino acid sequences, the more similar are the higher order structures resulting from folding and assembly. Thus, the nucleic acid constructs can include polynucleotides that encode polypeptides that are at least about 90%, or 95%, 98%, or 99% identical to one of SEQ ID NO: 1 with respect to amino acid sequence.

DNA sequences encoding an immunogenic gp120 polypeptide can be expressed in vitro by DNA transfer into a suitable host cell. The cell may be prokaryotic or eukaryotic. The term also includes any progeny of the subject host cell. It is understood that all progeny may not be identical to the parental cell since there may be mutations that occur during replication. Methods of stable transfer, meaning that the foreign DNA is continuously maintained in the host, are known in the art.

The polynucleotide sequences encoding an immunogenic gp120 polypeptide can be inserted into an expression vector including, but not limited to, a plasmid, virus or other vehicle that can be manipulated to allow insertion or incorporation of sequences and can be expressed in either prokaryotes or eukaryotes. Hosts can include microbial, yeast, insect, and mammalian organisms. Methods of expressing DNA sequences having eukaryotic or viral sequences in prokaryotes are well known in the art. Biologically functional viral and plasmid DNA vectors capable of expression and replication in a host are known in the art.

Transformation of a host cell with recombinant DNA can be carried out by conventional techniques that are well known to those of ordinary skill in the art. Where the host is prokaryotic, such as E. coli, competent cells which are capable of DNA uptake can be prepared from cells harvested after exponential growth phase and subsequently treated by the CaCl₂ method using procedures well known in the art. Alternatively, MgCl₂ or RbCl can be used. Transformation can also be performed after forming a protoplast of the host cell if desired, or by electroporation.

When the host is a eukaryote, such methods of transfection of DNA as calcium phosphate coprecipitates, conventional mechanical procedures such as microinjection, electroporation, insertion of a plasmid encased in liposomes, or virus vectors can be used. Eukaryotic cells can also be co-transformed with polynucleotide sequences encoding an immunogenic gp120 polypeptide, and a second foreign DNA molecule encoding a selectable phenotype, such as the herpes simplex thymidine kinase gene. Another method is to use a eukaryotic viral vector, such as simian virus 40 (SV40) or bovine papilloma virus, to transiently infect or transform eukaryotic cells and express the protein (see for example, Eukaryotic Viral Vectors, Cold Spring Harbor Laboratory, Gluzman ed., 1982).

IV. Immunogenic Compositions and Therapeutic Methods

Any of the gp120 polypeptides and nucleic acid molecules encoding the gp120 polypeptides disclosed herein can be used as immunogens, or to produce immunogens to elicit an immune response (immunogenic compositions) to gp120 such as to a gp120 expressing virus, for example to reduce HIV-I infection or a symptom of HIV-I infection. Following administration of a therapeutically effective amount of the disclosed therapeutic compositions, the subject can be monitored for HIV-I infection, symptoms associated with HIV-I infection, or both. Disclosed herein are methods of administering the therapeutic molecules disclosed herein (such as gp120 polypeptides and nucleic acids encoding gp120 polypeptides) to reduce HIV-I infection. In one example, a therapeutically effective amount of a gp120 polypeptide including SEQ ID NO: 1 or immunogenic fragment thereof is administered to a subject.

In certain embodiments, the immunogenic composition includes an adjuvant. An adjuvant can be a suspension of minerals, such as alum, aluminum hydroxide, aluminum phosphate, on which antigen is adsorbed; or water-in-oil emulsion in which antigen solution is emulsified in oil (MF-59, Freund's incomplete adjuvant), sometimes with the inclusion of killed mycobacteria (Freund's complete adjuvant) to further enhance antigenicity (inhibits degradation of antigen and/or causes influx of macrophages). In one embodiment, the adjuvant is a mixture of stabilizing detergents, micelle-forming agent, and oil available under the name PROVAX® (IDEC Pharmaceuticals, San Diego, Calif.). An adjuvant can also be an immunostimulatory nucleic acid, such as a nucleic acid including a CpG motif.

In one example, the immunogenic composition is mixed with an adjuvant containing two or more of a stabilizing detergent, a micelle-forming agent, and an oil. Suitable stabilizing detergents, micelle-forming agents, and oils are detailed in U.S. Pat. No. 5,585,103; U.S. Pat. No. 5,709,860; U.S. Pat. No. 5,270,202; and U.S. Pat. No. 5,695,770, all of which are incorporated by reference herein in their entirety. A stabilizing detergent is any detergent that allows the components of the emulsion to remain as a stable emulsion. Such detergents include polysorbate, 80 (TWEEN) (Sorbitan-mono-9-octadecanoate-poly(oxy-1,2-ethanediyl; manufactured by ICI Americas, Wilmington, Del.), TWEEN 40™, TWEEN 20™, TWEEN 60, ZWITTERGENT™ 3-12, TEEPOL HB7™, and SPAN 85™. These detergents are usually provided in an amount of approximately 0.05 to 0.5%, such as at about 0.2%. A micelle forming agent is an agent which is able to stabilize the emulsion formed with the other components such that a micelle-like structure is formed. Such agents generally cause some irritation at the site of injection in order to recruit macrophages to enhance the cellular response. Examples of such agents include polymer surfactants described by BASF Wyandotte publications, for example, Schmolka, J. Am. Oil. Client. Soc. 54:110, 1977, and Hunter et al., J. Immunol 129:1244, 1981, PLURONIC™ L62LF, L101, and L64, PEG1000, and TETRONIC™ 1501, 150R1, 701, 901, 1301, and 130R1. The chemical structures of such agents are well known in the art. In one embodiment, the agent is chosen to have a hydrophile-lipophile balance (HLB) of between 0 and 2, as defined by Hunter and Bennett, J. Immun. 133:3167, 1984. The agent can be provided in an effective amount, for example between 0.5 and 10%, or in an amount between 1.25 and 5%.

The oil included in the composition is chosen to promote the retention of the antigen in oil-in-water emulsion, to provide a vehicle for the desired antigen, and preferably has a melting temperature of less than 65° C. such that emulsion is formed either at room temperature (about 20° C. to 25° C.), or once the temperature of the emulsion is brought down to room temperature. Examples of such oils include squalene, Squalane, EICOSANE™, tetratetracontane, glycerol, and peanut oil or other vegetable oils. In one specific, non-limiting example, the oil is provided in an amount between 1 and 10%, or between 2.5 and 5%. The oil should be both biodegradable and biocompatible so that the body can break down the oil over time, and so that no adverse affects, such as granulomas, are evident upon use of the oil.

Immunogenic compositions can be formulated with an appropriate solid or liquid carrier, depending upon the particular mode of administration chosen. If desired, the disclosed pharmaceutical compositions can also contain minor amounts of non-toxic auxiliary substances, such as wetting or emulsifying agents, preservatives, and pH buffering agents and the like, for example sodium acetate or sorbitan monolaurate. Excipients that can be included in the disclosed compositions include flow conditioners and lubricants, for example silicic acid, talc, stearic acid or salts thereof, such as magnesium or calcium stearate, and/or polyethylene glycol, or derivatives thereof.

Immunogenic compositions can be provided as parenteral compositions, such as for injection or infusion. Such compositions are formulated generally by mixing a disclosed therapeutic agent at the desired degree of purity, in a unit dosage injectable form (solution, suspension, or emulsion), with a pharmaceutically acceptable carrier, for example one that is non-toxic to recipients at the dosages and concentrations employed and is compatible with other ingredients of the formulation. In addition, a disclosed therapeutic agent can be suspended in an aqueous carrier, for example, in an isotonic buffer solution at a pH of about 3.0 to about 8.0, preferably at a pH of about 3.5 to about 7.4, 3.5 to 6.0, or 3.5 to about 5.0. Useful buffers include sodium citrate-citric acid and sodium phosphate-phosphoric acid, and sodium acetate/acetic acid buffers. The active ingredient, optionally together with excipients, can also be in the form of a lyophilisate and can be made into a solution prior to parenteral administration by the addition of suitable solvents. Solutions such as those that are used, for example, for parenteral administration can also be used as infusion solutions.

A form of repository or “depot” slow release preparation can be used so that therapeutically effective amounts of the preparation are delivered into the bloodstream over many hours or days following transdermal injection or delivery. Such long acting formulations can be administered by implantation (for example subcutaneously or intramuscularly) or by intramuscular injection. The compounds can be formulated with suitable polymeric or hydrophobic materials (for example as an emulsion in an acceptable oil) or ion exchange resins, or as sparingly soluble derivatives, for example, as a sparingly soluble salt.

Immunogenic compositions that include a disclosed therapeutic agent can be delivered by way of a pump (see Langer, supra; Sefton, CRC Crit. Ref. Biomed. Eng. 14:201, 1987; Buchwald et al., Surgery 88:507, 1980; Saudek et al., N. Engl. J. Med. 321:574, 1989) or by continuous subcutaneous infusions, for example, using a mini-pump. An intravenous bag solution can also be employed. One factor in selecting an appropriate dose is the result obtained, as measured by the methods disclosed here, as are deemed appropriate by the practitioner. Other controlled release systems are discussed in Langer (Science 249:1527-33, 1990).

In one example, a pump is implanted (for example see U.S. Pat. Nos. 6,436,091; 5,939,380; and 5,993,414). Implantable drag infusion devices are used to provide patients with a constant and long-term dosage or infusion of a therapeutic agent. Such device can be categorized as either active or passive.

Active drug or programmable infusion devices feature a pump or a metering system to deliver the agent into the patient's system. An example of such an active infusion device currently available is the Medtronic SYNCHROMED™ programmable pump. Passive infusion devices, in contrast, do not feature a pump, but rather rely upon a pressurized drug reservoir to deliver the agent of interest. An example of such a device includes the Medtronic ISOMED™.

In particular examples, immunogenic compositions including a disclosed therapeutic agent are administered by sustained-release systems. Suitable examples of sustained-release systems include suitable polymeric materials (such as, semi-permeable polymer matrices in the form of shaped articles, for example films, or microcapsules), suitable hydrophobic materials (for example as an emulsion in an acceptable oil) or ion exchange resins, and sparingly soluble derivatives (such as, for example, a sparingly soluble salt). Sustained-release compositions can be administered orally, parenterally, intracistemally, intraperitoneally, topically (as by powders, ointments, gels, drops or transdermal patch), or as an oral or nasal spray. Sustained-release matrices include polylactides (U.S. Pat. No. 3,773,919, EP 58,481), copolymers of L-glutamic acid and gamma-ethyl-L-glutamate (Sidman et al., Biopolymers 22:547-556, 1983, poly(2-hydroxyethyl methacrylate)); (Langer et al., J. Biomed. Mater. Res. 15:167-277, 1981; Langer, Chem. Tech. 12:98-105, 1982, ethylene vinyl acetate (Langer et al., Id.) or poly-D-(−)-3-hydroxybutyric acid (EP 133,988).

Polymers can be used for ion-controlled release. Various degradable and nondegradable polymeric matrices for use in controlled drug delivery are known in the art (Langer, Accounts Chem. Res. 26:537, 1993). For example, the block copolymer, polaxamer 407 exists as a viscous yet mobile liquid at low temperatures but forms a semisolid gel at body temperature. It has shown to be an effective vehicle for formulation and sustained delivery of recombinant interleukin-2 and urease (Johnston et al., Pharm. Res. 9:425, 1992; and Pec, J. Parent. Sci. Tech. 44(2):58, 1990). Alternatively, hydroxyapatite has been used as a microcarrier for controlled release of proteins (Ijntema et al., Int. J. Pharm. 112:215, 1994). In yet another aspect, liposomes are used for controlled release as well as drug targeting of the lipid-capsulated drug (Betageri et al., Liposome Drug Delivery Systems, Technomic Publishing Co., Inc., Lancaster, Pa., 1993). Numerous additional systems for controlled delivery of therapeutic proteins are known (for example, U.S. Pat. No. 5,055,303; U.S. Pat. No. 5,188,837; U.S. Pat. No. 4,235,871; U.S. Pat. No. 4,501,728; U.S. Pat. No. 4,837,028; U.S. Pat. No. 4,957,735; and U.S. Pat. No. 5,019,369; U.S. Pat. No. 5,055,303; U.S. Pat. No. 5,514,670; U.S. Pat. No. 5,413,797; U.S. Pat. No. 5,268,164; U.S. Pat. No. 5,004,697; U.S. Pat. No. 4,902,505; U.S. Pat. No. 5,506,206; U.S. Pat. No. 5,271,961; U.S. Pat. No. 5,254,342; and U.S. Pat. No. 5,534,496).

Immunogenic compositions can be administered for therapeutic treatments. In therapeutic applications, a therapeutically effective amount of the immunogenic composition is administered to a subject suffering from a disease, such as HIV-I infection or AIDS. The immunogenic composition can be administered by any means known to one of skill in the art (see Banga, A., “Parenteral Controlled Delivery of Therapeutic Peptides and Proteins,” in Therapeutic Peptides and Proteins, Technomic Publishing Co., Inc., Lancaster, Pa., 1995) such as by intramuscular, subcutaneous, or intravenous injection, but even oral, nasal, or anal administration is contemplated. To extend the time during which the peptide or protein is available to stimulate a response, the peptide or protein can be provided as an implant, an oily injection, or as a particulate system. The particulate system can be a microparticle, a microcapsule, a microsphere, a nanocapsule, or similar particle (see, for example, Banga, supra). A particulate carrier based on a synthetic polymer has been shown to act as an adjuvant to enhance the immune response, in addition to providing a controlled release. Aluminum salts can also be used as adjuvants to produce an immune response.

Immunogenic compositions can be formulated in unit dosage form, suitable for individual administration of precise dosages. In pulse doses, a bolus administration of an immunogenic composition that includes a disclosed immunogen is provided, followed by a time-period wherein no disclosed immunogen is administered to the subject, followed by a second bolus administration. A therapeutically effective amount of an immunogenic composition can be administered in a single dose, or in multiple doses, for example daily, during a course of treatment. In specific, non-limiting examples, pulse doses of an immunogenic composition that include a disclosed immunogen are administered during the course of a day, during the course of a week, or during the course of a month.

Immunogenic compositions can be administered whenever the effect (such as decreased signs, symptom, or laboratory results of HIV-I infection) is desired. Generally, the dose is sufficient to treat or ameliorate symptoms or signs of disease without producing unacceptable toxicity to the subject. Systemic or local administration can be utilized.

Amounts effective for therapeutic use can depend on the severity of the disease and the age, weight, general state of the patient, and other clinical factors. Thus, the final determination of the appropriate treatment regimen will be made by the attending clinician. Typically, dosages used in vitro can provide useful guidance in the amounts useful for in situ administration of the pharmaceutical composition, and animal models may be used to determine effective dosages for treatment of particular disorders. Various considerations are described, for example in Gilman et al., eds., Goodman and Gilman: The Pharmacological Bases of Therapeutics, 8th ed., Pergamon Press, 1990; and Remington's Pharmaceutical Sciences, 17th ed., Mack Publishing Co., Easton, Pa., 1990. Typically, the dose range for a gp120 polypeptide is from about 0.1 μg/kg body weight to about 100 mg/kg body weight. Other suitable ranges include doses of from about 1 μg/kg to 10 mg/kg body weight. In one example, the dose is about 1.0 μg to about 50 mg, for example, 1 μg to 1 mg, such as 1 mg peptide per subject. The dosing schedule can vary from daily to as seldom as once a year, depending on clinical factors, such as the subject's sensitivity to the peptide and tempo of their disease. Therefore, a subject can receive a first dose of a disclosed therapeutic molecule, and then receive a second dose (or even more doses) at some later time(s), such as at least one day later, such as at least one week later.

The pharmaceutical compositions disclosed herein can be prepared and administered in dose units. Solid dose units include tablets, capsules, transdermal delivery systems, and suppositories. The administration of a therapeutic amount can be carried out both by single administration in the form of an individual dose unit or else several smaller dose units and also by multiple administrations of subdivided doses at specific intervals. Suitable single or divided doses include, but are not limited to about 0.01, 0.1, 0.5, 1, 3, 5, 10, 15, 30, or 50 μg protein/kg/day

The nucleic acid constructs encoding antigenic gp120 polypeptides described herein are used, for example, in combination, as pharmaceutical compositions (medicaments) for use in therapeutic, for example, prophylactic regimens (such as vaccines) and administered to subjects (for example, primate subjects such as human subjects) to elicit an immune response against one or more clade or strain of HIV. For example, the compositions described herein can be administered to a human (or non-human) subject prior to infection with HIV to inhibit infection by or replication of the virus. Thus, the pharmaceutical compositions described above can be administered to a subject to elicit a protective immune response against HIV. To elicit an immune response, a therapeutically effective (for example, immunologically effective) amount of the nucleic acid constructs are administered to a subject, such as a human (or non-human) subject.

Immunization by nucleic acid constructs is well known in the art and taught, for example, in U.S. Pat. No. 5,643,578 (which describes methods of immunizing vertebrates by introducing DNA encoding a desired antigen to elicit a cell-mediated or a humoral response), and U.S. Pat. No. 5,593,972 and U.S. Pat. No. 5,817,637 (which describe operably linking a nucleic acid sequence encoding an antigen to regulatory sequences enabling expression). U.S. Pat. No. 5,880,103 describes several methods of delivery of nucleic acids encoding immunogenic peptides or other antigens to an organism. The methods include liposomal delivery of the nucleic acids (or of the synthetic peptides themselves), and immune-stimulating constructs, or ISCOMS™, negatively charged cage-like structures of 30-40 nm in size formed spontaneously on mixing cholesterol and QUIL A™ (saponin).

For administration of gp120 nucleic acid molecules, the nucleic acid can be delivered intracellularly, for example by expression from an appropriate nucleic acid expression vector which is administered so that it becomes intracellular, such as by use of a retroviral vector (see U.S. Pat. No. 4,980,286), or by direct injection, or by use of microparticle bombardment (such as a gene gun; Biolistic, Dupont), or coating with lipids or cell-surface receptors or transfecting agents, or by administering it in linkage to a homeobox-like peptide which is known to enter the nucleus (for example Joliot et al., Proc, Natl. Acad. Sci. USA 1991, 88:1864-8). The present disclosure includes all forms of nucleic acid delivery, including synthetic oligos, naked DNA, plasmid and viral, integrated into the genome or not.

In another approach to using nucleic acids for immunization, an immunogenic gp120 polypeptide can also be expressed by attenuated viral hosts or vectors or bacterial vectors. Recombinant vaccinia virus, adeno-associated virus (AAV), herpes virus, retrovirus, or other viral vectors can be used to express the peptide or protein, thereby eliciting a CTL response. For example, vaccinia vectors and methods useful in immunization protocols are described in U.S. Pat. No. 4,722,848. BCG (Bacillus Calmette Guerin) provides another vector for expression of the peptides (see Stover, Nature 351:456-460, 1991).

In one example, a viral vector is utilized. These vectors include, but are not limited to, adenovirus, herpes virus, vaccinia, or an RNA virus such as a retrovirus. In one example, the retroviral vector is a derivative of a murine or avian retrovirus. Examples of retroviral vectors in which a single foreign gene can be inserted include, but are not limited to: Moloney murine leukemia virus (MoMuLV), Harvey murine sarcoma virus (HaMuSV), murine mammary tumor virus (MuMTV), and Rous Sarcoma Virus (RSV). When the subject is a human, a vector such as the gibbon ape leukemia virus (GaLV) can be utilized. A number of additional retroviral vectors can incorporate multiple genes. All of these vectors can transfer or incorporate a gene for a selectable marker so that transduced cells can be identified and generated. By inserting a nucleic acid sequence encoding a gp120 polypeptide into the viral vector, along with another gene that encodes the ligand for a receptor on a specific target cell, for example, the vector is now target specific. Retroviral vectors can be made target specific by attaching, for example, a sugar, a glycolipid, or a protein. Preferred targeting is accomplished by using an antibody to target the retroviral vector. Those of skill in the art will know of, or can readily ascertain without undue experimentation, specific polynucleotide sequences which can be inserted into the retroviral genome or attached to a viral envelope to allow target specific delivery of the retroviral vector containing the polynucleotide encoding a gp120 polypeptide.

Since recombinant retroviruses are defective, they need assistance in order to produce infectious vector particles. This assistance can be provided, for example, by using helper cell lines that contain plasmids encoding all of the structural genes of the retrovirus under the control of regulatory sequences within the LTR. These plasmids are missing a nucleotide sequence that enables the packaging mechanism to recognize an RNA transcript for encapsidation. Helper cell lines that have deletions of the packaging signal include, but are not limited to Q2, PA317, and PA12, for example. These cell lines produce empty virions, since no genome is packaged. If a retroviral vector is introduced into such cells in which the packaging signal is intact, but the structural genes are replaced by other genes of interest, the vector can be packaged and vector virion produced.

Suitable formulations for the nucleic acid constructs, include aqueous and non-aqueous solutions, isotonic sterile solutions, which can contain anti-oxidants, buffers, and bacteriostats, and aqueous and non-aqueous sterile suspensions that can include suspending agents, solubilizers, thickening agents, stabilizers, and preservatives. The formulations can be presented in unit-dose or multi-dose sealed containers, such as ampules and vials, and can be stored in a freeze-dried (lyophilized) condition requiring only the addition of the sterile liquid carrier, for example, water, immediately prior to use. Extemporaneous solutions and suspensions can be prepared from sterile powders, granules, and tablets. Preferably, the carrier is a buffered saline solution. More preferably, the composition for use in the inventive method is formulated to protect the nucleic acid constructs from damage prior to administration. For example, the composition can be formulated to reduce loss of the adenoviral vectors on devices used to prepare, store, or administer the expression vector, such as glassware, syringes, or needles. The compositions can be formulated to decrease the light sensitivity and/or temperature sensitivity of the components. To this end, the composition preferably comprises a pharmaceutically acceptable liquid carrier, such as, for example, those described above, and a stabilizing agent selected from the group consisting of polysorbate 80, L-arginine, polyvinylpyrrolidone, trehalose, and combinations thereof.

In therapeutic applications, a therapeutically effective amount of the composition is administered to a subject prior to or following exposure to or infection by HIV. When administered prior to exposure, the therapeutic application can be referred to as a prophylactic administration (such as in the form of a vaccine). Single or multiple administrations of the compositions are administered depending on the dosage and frequency as required and tolerated by the subject. In one embodiment, the dosage is administered once as a bolus, but in another embodiment can be applied periodically until a therapeutic result, such as a protective immune response, is achieved. Generally, the dose is sufficient to treat or ameliorate symptoms or signs of disease without producing unacceptable toxicity to the subject. Systemic or local administration can be utilized.

In the context of nucleic acid vaccines, naturally occurring or synthetic immunostimulatory compositions that bind to and stimulate receptors involved in innate immunity can be administered along with nucleic acid constructs encoding the gp120 polypeptides. For example, agents that stimulate certain Toll-like receptors (such as TLR7, TLR8 and TLR9) can be administered in combination with the nucleic acid constructs encoding gp120 polypeptides. In some embodiments, the nucleic acid construct is administered in combination with immunostimulatory CpG oligonucleotides.

Nucleic acid constructs encoding gp120 polypeptides can be introduced in vivo as naked DNA plasmids. DNA vectors can be introduced into the desired host cells by methods known in the art, including but not limited to transfection, electroporation (for example, transcutaneous electroporation), microinjection, transduction, cell fusion, DEAE dextran, calcium phosphate precipitation, use of a gene gun, or use of a DNA vector transporter (See for example, Wu et al. J. Biol. Chem., 267:963-967, 1992; Wu and Wu J. Biol. Chem., 263:14621-14624, 1988; and Williams et al. Proc. Natl. Acad. Sci. USA 88:2726-2730, 1991). As described in detail in the Examples, a needleless delivery device, such as a BIOJECTOR® needleless injection device can be utilized to introduce the therapeutic nucleic acid constructs in vivo. Receptor-mediated DNA delivery approaches can also be used (Curiel et al. Hum. Gene Ther., 3:147-154, 1992; and Wu and Wu, J. Biol. Chem., 262:4429-4432, 1987). Methods for formulating and administering naked DNA to mammalian muscle tissue are disclosed in U.S. Pat. Nos. 5,580,859 and 5,589,466, both of which are herein incorporated by reference. Other molecules are also useful for facilitating transfection of a nucleic acid in vivo, such as a cationic oligopeptide (for example, WO95/21931), peptides derived from DNA binding proteins (for example, WO96/25508), or a cationic polymer (for example, WO95/21931).

Another well known method that can be used to introduce nucleic acid constructs encoding gp120 immunogens into host cells is particle bombardment (also know as biolistic transformation). Biolistic transformation is commonly accomplished in one of several ways. One common method involves propelling inert or biologically active particles at cells. This technique is disclosed in, for example, U.S. Pat. Nos. 4,945,050, 5,036,006; and 5,100,792, all to Sanford et al., which are hereby incorporated by reference. Generally, this procedure involves propelling inert or biologically active particles at the cells under conditions effective to penetrate the outer surface of the cell and to be incorporated within the interior thereof. When inert particles are utilized, the plasmid can be introduced into the cell by coating the particles with the plasmid containing the exogenous DNA. Alternatively, the target cell can be surrounded by the plasmid so that the plasmid is carried into the cell by the wake of the particle.

Alternatively, the vector can be introduced in vivo by lipofection. For the past decade, there has been increasing use of liposomes for encapsulation and transfection of nucleic acids in vitro. Synthetic cationic lipids designed to limit the difficulties and dangers encountered with liposome mediated transfection can be used to prepare liposomes for in vivo transfection of a gene encoding a marker (Felgner et. al. Proc. Natl. Acad. Sci. USA 84:7413-7417, 1987; Mackey, et al. Proc. Natl. Acad. Sci. USA 85:8027-8031, 1988; Ulmer et al. Science 259:1745-1748, 1993). The use of cationic lipids can promote encapsulation of negatively charged nucleic acids, and also promote fusion with negatively charged cell membranes (Felgner and Ringold Science 337:387-388, 1989). Particularly useful lipid compounds and compositions for transfer of nucleic acids are described in WO95/18863 and WO96/17823, and in U.S. Pat. No. 5,459,127, herein incorporated by reference.

As with the immunogenic polypeptide, the nucleic acid compositions may be administered in a single dose, or multiple doses separated by a time interval can be administered to elicit an immune response against HIV. For example, two doses, or three doses, or four doses, or five doses, or six doses or more can be administered to a subject over a period of several weeks, several months or even several years, to optimize the immune response.

It may be advantageous to administer the immunogenic compositions disclosed herein with other agents such as proteins, peptides, antibodies, and other anti-HIV agents. Examples of such anti-HIV therapeutic agents include nucleoside reverse transcriptase inhibitors, such as abacavir, AZT, didanosine, emtricitabine, lamivudine, stavudine, tenofovir, zalcitabine, zidovudine, and the like, non-nucleoside reverse transcriptase inhibitors, such as delavirdine, efavirenz, nevirapine, protease inhibitors such as amprenavir, atazanavir, indinavir, lopinavir, nelfinavir, osamprenavir, ritonavir, saquinavir, tipranavir, and the like, and fusion protein inhibitors such as enfuvirtide and the like. In certain embodiments, immunogenic compositions are administered concurrently with other anti-HIV therapeutic agents. In certain embodiments, the immunogenic compositions are administered sequentially with other anti-HIV therapeutic agents, such as before or after the other agent. One of ordinary skill in the art would know that sequential administration can mean immediately following or after an appropriate period of time, such as hours days, weeks, months, or even years later.

The immunogenic gp120 polypeptides and nucleic acid encoding these polypeptides (such as stabilized gp120 polypeptides) can be used in a novel multistep immunization regime. Typically, this regime includes administering to a subject a therapeutically effective amount of a gp120 polypeptide as disclosed herein (the prime) and boosting the immunogenic response with stabilized gp140 trimer (Yang et al. J Virol. 76(9):4634-42, 2002) after an appropriate period of time. The method of eliciting such an immune reaction is what is known as “prime-boost.” In this method, a gp120 polypeptide is initially administered to a subject and at periodic times thereafter stabilized gp140 trimer boosts are administered. Examples of stabilized gp140 or gp120 trimers can be found for example in U.S. Pat. No. 6,911,205 which is incorporated herein in its entirely.

The prime can be administered as a single dose or multiple doses, for example two doses, three doses, four doses, five doses, six doses or more can be administered to a subject over day week or months. The boost can be administered as a single dose or multiple doses, for example two to six doses, or more can be administered to a subject over a day, a week or months. Multiple boosts can also be given, such one to five, or more.

The boosts can be an identical molecule or a somewhat different, but related, molecule. For example, one preferred strategy with the present disclosure would be to prime using a stabilized gp120 polypeptide and boosting periodically with stabilized trimers where the gp120 units are designed to come closer and closer to the wild type gp120 over the succession of boosts. For example, the first prime could be a stabilized gp120 polypeptide, with a boost by a stabilized trimer form with the same stabilized gp120 or a trimer with less deletions or changes from the native gp120 conformation, with subsequent boosts using trimers that had still less deletions or changes from the native gp120 conformation until the boosts were finally being given by trimers with a gp120 portion based on the native wild type HIV gp120.

One can also use cocktails containing a variety of different HIV strains to prime and boost with trimers from a variety of different HIV strains or with trimers that are a mixture of multiple HIV strains. For example, the first prime could be with a gp120 polypeptide from one primary HIV isolate, with subsequent boosts using trimers from different primary isolates.

In certain embodiments, the prime is a nucleic acid construct comprising a nucleic acid sequence encoding a gp120 immunogen as disclosed herein, for example an nucleotide sequence encoding the amino acid sequence set forth as SEQ ID NO: 1. In certain embodiments the boost comprises a nucleic acid sequence encoding a stabilized gp140 trimer.

V. Crystal Structures

The stabilized gp120 polypeptides disclosed herein can be used to produce detailed models of gp120 polypeptide atomic structure. Exemplary coordinate data is given in Table 1. The atomic coordinate data is disclosed herein, or the coordinate data derived from homologous proteins may be used to build a three-dimensional model of a gp120 polypeptide or a portion thereof, for example by providing a sufficient number of atoms of the stabilized form of gp120 as defined by the coordinates of Table 1 which represent a surface or three-dimensional region of interest, such as an antigenic surface or ligand binding site. Thus, there can be provided the coordinates of at least about 5, such at least about 10, at least about 20, at least about 30, at least at least about 40, at least about 50, at least about 60, at least about 70, at least about 80, at least about 90, at least about 100, at least about 150, at least about 200, at least about 250, at least about 300, at least about 350, at least about 400, at least about 450, at least about 500 or more atoms of the structure, such as defined by the coordinates of Table 1. Thus, a sub-domain, region, or fragment of interest of the stabilized form of gp120 or the gp120 with the extended V3 loop which is in the vicinity of the antigenic surface, can be provided for identifying or rationally designing a compound or drug, such as an immunogen. A “sub-domain,” “region,” or “fragment” can mean at least one, for example, one, two, three, four, or more, element(s) of secondary structure of particular regions of the stabilized form of gp120, and includes those set forth in Table 1.

Any available computational methods may be used to build the three dimensional model. As a starting point, the X-ray diffraction pattern obtained from the assemblage of the molecules or atoms in a crystalline version of a gp120 polypeptide can be used to build an electron density map using tools well known to those skilled in the art of crystallography and X-ray diffraction techniques. Additional phase information extracted either from the diffraction data and available in the published literature and/or from supplementing experiments may then used to complete the reconstruction.

For an overview of the procedures of collecting, analyzing, and utilizing X-ray diffraction data for the construction of electron densities see, for example, Campbell et al., Biological Spectroscopy, The Benjamin/Cummings Publishing Co., Inc., Menlo Park, Calif., 1984; Cantor et al., Biophysical Chemistry, Part II: Techniques for the study of biological structure and function, W.H. Freeman and Co., San Francisco, Calif. 1980; A. T. Brunger, X-plor Version 3.1: A system for X-ray crystallography and NMR, Yale Univ. Pr., New Haven, Conn. 1993; M. M. Woolfson, An Introduction to X-ray Crystallography, Cambridge Univ. Pr., Cambridge, UK, 1997; J. Drenth, Principles of Protein X-ray Crystallography (Springer Advanced Texts in Chemistry), Springer Verlag; Berlin, 1999; Tsirelson et al, Electron Density and Bonding in Crystals: Principles, Theory and X-ray Diffraction Experiments in Solid State Physics and Chemistry, Inst. of Physics Pub., 1996; each of which is herein specifically incorporated by reference in their entirety.

Information on molecular modeling can be found for example in, M. Schlecht, Molecular Modeling on the PC, 1998, John Wiley & Sons; Gans et al., Fundamental Principals of Molecular Modeling, Plenum Pub. Corp., 1996; N. C. Cohen (editor), Guidebook on Molecular Modeling in Drug Design, Academic Press, 1996; and W. B. Smith, Introduction to Theoretical Organic Chemistry and Molecular Modeling, 1996.

Typically, a well-ordered crystal that will diffract x-rays strongly is used to solve the three-dimensional structure of a protein by x-ray crystallography. The crystallographic method directs a beam of x-rays onto a regular, repeating array of many identical molecules. The x-rays are diffracted from it in a pattern from which the atomic positions of the atom that make up the molecule of interest can be determined.

Substantially pure and homogeneous protein samples are usually used for crystallization. Typically, crystals form when molecules are precipitated very slowly from supersaturated solutions. A typical procedure for making protein crystals is the hanging-drop method, in which a drop of protein solution is brought very gradually to supersaturation by loss of water from the droplet to the larger reservoir that contains salt, polyethylene glycol, or other solution that functions as a hydroattractant, although any other method that generates diffraction quality crystals can be used. In some examples diffraction quality crystals are obtained by seeding the supersaturated solution with smaller crystals that serve as templates.

Powerful x-ray beams can be produced from synchrotron storage rings where electrons (or positrons) travel close to the speed of light. These particles emit very strong radiation at all wavelengths from short gamma rays to visible light. When used as an x-ray source, only radiation within a window of suitable wavelengths is channeled from the storage ring.

In diffraction experiments a narrow and parallel beam of x-rays is taken out from the x-ray source and directed onto the crystal to produce diffracted beams. The incident x-ray beam causes damage to both protein and solvent molecules. The crystal is, therefore, usually cooled to prolong its lifetime (for example to −220° to −50° C.). In some examples, single crystals are used to obtain a data set, while in other examples, multiple crystals are used to obtain a data set. The x-ray beam must strike the crystal from many different directions to produce all possible diffraction spots, thereby creating a complete data set. Therefore, the crystal is rotated relative to the beam during data collection. The diffracted spots are recorded either on a film, or by an electronic detector, both of which are commercially available.

When the primary beam from an x-ray source strikes the crystal, x-rays interact with the electrons on each atom in the crystal and cause them to oscillate. The oscillating electrons serve as a new source of x-rays, which are emitted in almost all directions in a process referred to as scattering. When atoms (and hence their electrons) are arranged in a regular three-dimensional array, as in a crystal, the x-rays emitted from the oscillating electrons interfere with one another. In most cases, these x-rays, colliding from different directions, cancel each other out; those from certain directions, however, will add together to produce diffracted beams of radiation that can be recorded as a pattern on a photographic plate or detector.

The diffraction pattern obtained in an x-ray experiment is related to the crystal that caused the diffraction. X-rays that are reflected from adjacent planes travel different distances, and diffraction only occurs when the difference in distance is equal to the wavelength of the x-ray beam. This distance is dependent on the reflection angle, which is equal to the angle between the primary beam and the planes.

Each atom in a crystal scatters x-rays in all directions, and only those that positively interfere with one another, according to Bragg's law (2d sin θ=λ), give rise to diffracted beams that can be recorded as a distinct diffraction spot above background. Each diffraction spot is the result of interference of all x-rays with the same diffraction angle emerging from all atoms. To extract information about individual atoms from such a system requires considerable computation. The mathematical tool that is used to handle such problems is called the Fourier transform.

Each diffracted beam, which is recorded as a spot on the film, is defined by three properties: the amplitude, which is measured as the intensity of the spot; the wavelength, which is determined by the x-ray source; and the phase information, which is lost in x-ray experiments and must be calculated. All three properties are used for all of the diffracted beams, in order to determine the position of the atoms giving rise to the diffracted beams. Methods of determining the phases are well know in the art.

For example, phase differences between diffracted spots can be determined from intensity changes following heavy atom derivatization. Another example would be determining the phases by molecular replacement.

The amplitudes and the phases of the diffraction data from the protein crystals are used to calculate an electron-density map of the repeating unit of the crystal. A model of the particular amino acid sequence is built to approximate the electron density map.

The initial model will contain some errors. Provided the protein crystals diffract to high enough resolution (e.g., better than 3.5 Å), most or substantially all of the errors can be removed by crystallographic refinement of the model using computer algorithms. In this process, the model is changed to minimize the difference between the experimentally observed diffraction amplitudes and those calculated for a hypothetical crystal containing the model. This difference is expressed as an R factor (residual disagreement) which is 0.0 for exact agreement and about 0.59 for total disagreement.

Typically, the R factor of a refined model is preferably between 0.15 and 0.35 (such as less than about 0.24-0.28) for a well-determined protein structure. The residual difference is a consequence of errors and imperfections in the data. These derive from various sources, including slight variations in the conformation of the protein molecules, as well as inaccurate corrections both for the presence of solvent and for differences in the orientation of the microcrystals from which the crystal is built. Thus, the final model represents an average of molecules that are slightly different both in conformation and orientation.

In refined structures at high resolution, there are usually no major errors in the orientation of individual residues, and the estimated errors in atomic positions are usually around 0.1-0.2 Å, provided the amino acid sequence is known.

Most x-ray structures are determined to a resolution between 1.7 Å. and 3.5 Å. Electron-density maps with this resolution range are preferably interpreted by fitting the known amino acid sequences into regions of electron density in which individual atoms are not resolved.

VI. Crystals Structure of Stabilized gp120 in Complex with the Antibody b12

The present disclosure also relates to the crystals obtained from a stabilized form of gp120 in complex with the b12 antibody, the crystal structures of a stabilized form of gp120 in complex with the b12 antibody, the three-dimensional coordinates of a stabilized form of gp120 polypeptide in complex with the b12 antibody and three-dimensional structures of models of a stabilized forms of gp120 in complex with the b12 antibody. The structure of a stabilized gp120 polypeptide was solved in complex with the b12 Fab. Analysis of the structure revealed the atomic level details of the interaction of gp120 and the neutralizing antibody b12. Table 1 provides the atomic coordinates of the crystal structure of the polypeptide encoded by SEQ ID NO: 1 in complex with the Fab portion of b12.

TABLE 1 The structural coordinates of an exemplary stabilized form of gp120 in complex with a neutralizing antibody at atomic resolution ATOM 1 N GLU G 83 123.254 169.146 272.753 1.00 104.89 ATOM 2 CA GLU G 83 122.496 168.519 273.875 1.00 104.53 ATOM 3 CB GLU G 83 123.433 167.698 274.764 1.00 104.93 ATOM 4 CG GLU G 83 124.008 166.461 274.090 1.00 103.74 ATOM 5 CD GLU G 83 124.974 165.704 274.982 1.00 103.23 ATOM 6 OE1 GLU G 83 125.371 164.580 274.611 1.00 97.65 ATOM 7 OE2 GLU G 83 125.336 166.234 276.054 1.00 102.28 ATOM 8 C GLU G 83 121.752 169.560 274.709 1.00 104.55 ATOM 9 O GLU G 83 120.783 169.237 275.399 1.00 104.96 ATOM 10 N VAL G 84 122.206 170.809 274.637 1.00 103.79 ATOM 11 CA VAL G 84 121.589 171.902 275.387 1.00 102.82 ATOM 12 CB VAL G 84 122.501 173.155 275.428 1.00 102.35 ATOM 13 CG1 VAL G 84 122.455 173.903 274.103 1.00 102.55 ATOM 14 CG2 VAL G 84 122.108 174.071 276.579 1.00 101.94 ATOM 15 C VAL G 84 120.218 172.257 274.806 1.00 102.14 ATOM 16 O VAL G 84 119.913 171.922 273.660 1.00 101.31 ATOM 17 N VAL G 85 119.395 172.929 275.605 1.00 101.48 ATOM 18 CA VAL G 85 118.034 173.263 275.198 1.00 100.62 ATOM 19 CB VAL G 85 116.985 172.519 276.069 1.00 100.91 ATOM 20 CG1 VAL G 85 117.278 172.708 277.554 1.00 101.24 ATOM 21 CG2 VAL G 85 115.571 172.974 275.727 1.00 100.59 ATOM 22 C VAL G 85 117.772 174.771 275.228 1.00 99.51 ATOM 23 O VAL G 85 117.932 175.420 276.263 1.00 99.53 ATOM 24 N LEU G 86 117.382 175.321 274.081 1.00 97.98 ATOM 25 CA LEU G 86 116.978 176.724 273.998 1.00 96.89 ATOM 26 CB LEU G 86 118.134 177.615 273.517 1.00 97.06 ATOM 27 CG LEU G 86 118.878 177.296 272.217 1.00 97.70 ATOM 28 CD1 LEU G 86 118.089 177.760 271.001 1.00 98.33 ATOM 29 CD2 LEU G 86 120.251 177.949 272.231 1.00 96.24 ATOM 30 C LEU G 86 115.738 176.889 273.120 1.00 95.79 ATOM 31 O LEU G 86 115.442 176.038 272.281 1.00 94.69 ATOM 32 N VAL G 87 115.017 177.988 273.323 1.00 94.62 ATOM 33 CA VAL G 87 113.739 178.205 272.649 1.00 93.65 ATOM 34 CB VAL G 87 112.605 178.454 273.668 1.00 93.65 ATOM 35 CG1 VAL G 87 112.293 177.182 274.438 1.00 93.22 ATOM 36 CG2 VAL G 87 112.980 179.580 274.622 1.00 94.66 ATOM 37 C VAL G 87 113.776 179.355 271.641 1.00 92.84 ATOM 38 O VAL G 87 114.832 179.688 271.099 1.00 92.96 ATOM 39 N ASN G 88 112.609 179.947 271.397 1.00 91.34 ATOM 40 CA ASN G 88 112.451 181.048 270.446 1.00 89.66 ATOM 41 CB ASN G 88 113.440 182.180 270.743 1.00 89.27 ATOM 42 CG ASN G 88 112.944 183.532 270.260 1.00 88.68 ATOM 43 OD1 ASN G 88 113.565 184.562 270.521 1.00 88.94 ATOM 44 ND2 ASN G 88 111.818 183.534 269.555 1.00 87.44 ATOM 45 C ASN G 88 112.560 180.589 268.990 1.00 88.91 ATOM 46 O ASN G 88 112.864 181.380 268.097 1.00 89.11 ATOM 47 N VAL G 89 112.305 179.303 268.764 1.00 88.11 ATOM 48 CA VAL G 89 112.288 178.737 267.418 1.00 87.07 ATOM 49 CB VAL G 89 113.688 178.231 266.983 1.00 86.99 ATOM 50 CG1 VAL G 89 114.260 177.256 268.008 1.00 87.84 ATOM 51 CG2 VAL G 89 113.626 177.598 265.599 1.00 86.60 ATOM 52 C VAL G 89 111.251 177.615 267.323 1.00 86.01 ATOM 53 O VAL G 89 111.348 176.601 268.016 1.00 85.96 ATOM 54 N THR G 90 110.252 177.812 266.468 1.00 84.75 ATOM 55 CA THR G 90 109.152 176.860 266.337 1.00 83.02 ATOM 56 CB THR G 90 107.810 177.580 266.078 1.00 83.44 ATOM 57 OG1 THR G 90 107.608 178.595 267.069 1.00 82.99 ATOM 58 CG2 THR G 90 106.649 176.594 266.126 1.00 82.76 ATOM 59 C THR G 90 109.408 175.852 265.221 1.00 82.17 ATOM 60 O THR G 90 109.967 176.191 264.177 1.00 81.57 ATOM 61 N GLU G 91 108.996 174.611 265.455 1.00 81.76 ATOM 62 CA GLU G 91 109.144 173.546 264.472 1.00 80.78 ATOM 63 CB GLU G 91 110.467 172.804 264.685 1.00 80.69 ATOM 64 CG GLU G 91 110.799 171.780 263.607 1.00 79.61 ATOM 65 CD GLU G 91 111.341 172.409 262.334 1.00 78.94 ATOM 66 OE1 GLU G 91 111.237 173.645 262.178 1.00 77.88 ATOM 67 OE2 GLU G 91 111.873 171.662 261.487 1.00 78.78 ATOM 68 C GLU G 91 107.970 172.576 264.571 1.00 80.07 ATOM 69 O GLU G 91 107.603 172.144 265.664 1.00 80.33 ATOM 70 N ASN G 92 107.382 172.242 263.426 1.00 78.73 ATOM 71 CA ASN G 92 106.231 171.344 263.393 1.00 76.82 ATOM 72 CB ASN G 92 105.410 171.554 262.115 1.00 77.01 ATOM 73 CG ASN G 92 106.276 171.762 260.885 1.00 76.17 ATOM 74 OD1 ASN G 92 107.417 171.303 260.825 1.00 72.36 ATOM 75 ND2 ASN G 92 105.732 172.459 259.893 1.00 74.12 ATOM 76 C ASN G 92 106.608 169.874 263.560 1.00 75.81 ATOM 77 O ASN G 92 107.632 169.418 263.049 1.00 76.30 ATOM 78 N PHE G 93 105.770 169.143 264.289 1.00 73.85 ATOM 79 CA PHE G 93 106.000 167.730 264.558 1.00 70.93 ATOM 80 CB PHE G 93 106.209 167.500 266.057 1.00 71.05 ATOM 81 CG PHE G 93 107.598 167.813 266.536 1.00 71.35 ATOM 82 CD1 PHE G 93 108.005 169.123 266.723 1.00 69.21 ATOM 83 CE1 PHE G 93 109.282 169.412 267.169 1.00 70.25 ATOM 84 CZ PHE G 93 110.165 168.384 267.442 1.00 70.26 ATOM 85 CE2 PHE G 93 109.770 167.073 267.267 1.00 69.52 ATOM 86 CD2 PHE G 93 108.493 166.792 266.818 1.00 71.29 ATOM 87 C PHE G 93 104.824 166.889 264.083 1.00 69.33 ATOM 88 O PHE G 93 103.682 167.344 264.086 1.00 69.00 ATOM 89 N ASN G 94 105.112 165.658 263.675 1.00 67.80 ATOM 90 CA ASN G 94 104.071 164.707 263.313 1.00 66.80 ATOM 91 CB ASN G 94 103.593 164.935 261.879 1.00 66.55 ATOM 92 CG ASN G 94 102.259 164.266 261.597 1.00 66.98 ATOM 93 OD1 ASN G 94 101.764 164.296 260.470 1.00 65.74 ATOM 94 ND2 ASN G 94 101.670 163.660 262.623 1.00 66.09 ATOM 95 C ASN G 94 104.559 163.276 263.493 1.00 65.95 ATOM 96 O ASN G 94 105.085 162.666 262.562 1.00 64.14 ATOM 97 N TRP G 95 104.368 162.747 264.698 1.00 65.96 ATOM 98 CA TRP G 95 104.875 161.427 265.063 1.00 67.53 ATOM 99 CB TRP G 95 104.642 161.158 266.555 1.00 66.95 ATOM 100 CG TRP G 95 103.214 160.852 266.927 1.00 67.29 ATOM 101 CD1 TRP G 95 102.115 161.624 266.681 1.00 67.04 ATOM 102 NE1 TRP G 95 100.987 161.016 267.181 1.00 66.67 ATOM 103 CE2 TRP G 95 101.345 159.833 267.772 1.00 61.94 ATOM 104 CD2 TRP G 95 102.741 159.697 267.635 1.00 65.11 ATOM 105 CE3 TRP G 95 103.363 158.559 268.161 1.00 62.98 ATOM 106 CZ3 TRP G 95 102.583 157.611 268.797 1.00 64.55 ATOM 107 CH2 TRP G 95 101.198 157.775 268.917 1.00 63.66 ATOM 108 CZ2 TRP G 95 100.562 158.876 268.413 1.00 62.16 ATOM 109 C TRP G 95 104.284 160.302 264.213 1.00 67.75 ATOM 110 O TRP G 95 104.639 159.135 264.380 1.00 69.72 ATOM 111 N CYS G 96 103.397 160.662 263.293 1.00 67.07 ATOM 112 CA CYS G 96 102.762 159.683 262.423 1.00 68.52 ATOM 113 CB CYS G 96 101.291 160.040 262.225 1.00 70.33 ATOM 114 SG CYS G 96 100.394 160.126 263.783 1.00 78.37 ATOM 115 C CYS G 96 103.473 159.572 261.080 1.00 66.87 ATOM 116 O CYS G 96 103.953 158.499 260.708 1.00 65.72 ATOM 117 N LYS G 97 103.542 160.687 260.359 1.00 64.83 ATOM 118 CA LYS G 97 104.243 160.739 259.083 1.00 63.71 ATOM 119 CB LYS G 97 104.089 162.127 258.460 1.00 64.26 ATOM 120 CG LYS G 97 103.982 162.140 256.942 1.00 63.41 ATOM 121 CD LYS G 97 102.583 161.752 256.487 1.00 61.25 ATOM 122 CE LYS G 97 102.350 162.122 255.030 1.00 61.28 ATOM 123 NZ LYS G 97 103.283 161.414 254.113 1.00 62.56 ATOM 124 C LYS G 97 105.724 160.426 259.290 1.00 63.95 ATOM 125 O LYS G 97 106.376 159.840 258.424 1.00 63.67 ATOM 126 N ASN G 98 106.243 160.811 260.453 1.00 62.11 ATOM 127 CA ASN G 98 107.648 160.609 260.780 1.00 61.31 ATOM 128 CB ASN G 98 108.276 161.924 261.249 1.00 60.28 ATOM 129 CG ASN G 98 108.190 163.021 260.201 1.00 60.31 ATOM 130 OD1 ASN G 98 107.961 164.187 260.524 1.00 49.62 ATOM 131 ND2 ASN G 98 108.371 162.650 258.937 1.00 58.01 ATOM 132 C ASN G 98 107.863 159.521 261.831 1.00 61.35 ATOM 133 O ASN G 98 108.546 159.741 262.833 1.00 61.27 ATOM 134 N ASP G 99 107.276 158.350 261.599 1.00 60.66 ATOM 135 CA ASP G 99 107.446 157.214 262.499 1.00 61.71 ATOM 136 CB ASP G 99 106.537 156.055 262.081 1.00 61.54 ATOM 137 CG ASP G 99 106.629 154.866 263.024 1.00 62.66 ATOM 138 OD1 ASP G 99 107.017 155.057 264.199 1.00 61.74 ATOM 139 OD2 ASP G 99 106.309 153.738 262.589 1.00 62.64 ATOM 140 C ASP G 99 108.908 156.778 262.497 1.00 61.94 ATOM 141 O ASP G 99 109.413 156.262 261.499 1.00 60.91 ATOM 142 N MET G 100 109.592 156.990 263.614 1.00 61.82 ATOM 143 CA MET G 100 111.031 156.768 263.640 1.00 63.61 ATOM 144 CB MET G 100 111.750 157.881 264.407 1.00 64.81 ATOM 145 CG MET G 100 111.536 157.878 265.904 1.00 66.39 ATOM 146 SD MET G 100 112.326 159.323 266.640 1.00 67.93 ATOM 147 CE MET G 100 113.946 159.235 265.901 1.00 40.62 ATOM 148 C MET G 100 111.464 155.387 264.132 1.00 62.32 ATOM 149 O MET G 100 112.659 155.116 264.226 1.00 65.26 ATOM 150 N VAL G 101 110.510 154.511 264.434 1.00 59.61 ATOM 151 CA VAL G 101 110.865 153.113 264.648 1.00 57.39 ATOM 152 CB VAL G 101 109.876 152.355 265.572 1.00 57.37 ATOM 153 CG1 VAL G 101 109.235 153.304 266.571 1.00 57.22 ATOM 154 CG2 VAL G 101 108.823 151.636 264.762 1.00 49.27 ATOM 155 C VAL G 101 110.933 152.460 263.273 1.00 56.44 ATOM 156 O VAL G 101 111.497 151.377 263.111 1.00 57.28 ATOM 157 N GLU G 102 110.370 153.153 262.285 1.00 53.90 ATOM 158 CA GLU G 102 110.400 152.716 260.895 1.00 56.12 ATOM 159 CB GLU G 102 109.466 153.585 260.052 1.00 56.01 ATOM 160 CG GLU G 102 108.829 152.874 258.870 1.00 62.83 ATOM 161 CD GLU G 102 107.626 152.034 259.267 1.00 68.84 ATOM 162 OE1 GLU G 102 106.616 152.057 258.532 1.00 70.76 ATOM 163 OE2 GLU G 102 107.686 151.356 260.316 1.00 70.94 ATOM 164 C GLU G 102 111.819 152.787 260.335 1.00 57.03 ATOM 165 O GLU G 102 112.098 152.253 259.263 1.00 56.92 ATOM 166 N GLN G 103 112.709 153.454 261.062 1.00 59.60 ATOM 167 CA GLN G 103 114.122 153.501 260.699 1.00 62.96 ATOM 168 CB GLN G 103 114.549 154.926 260.342 1.00 62.95 ATOM 169 CG GLN G 103 114.206 155.971 261.390 1.00 63.54 ATOM 170 CD GLN G 103 114.527 157.379 260.928 1.00 65.95 ATOM 171 OE1 GLN G 103 113.849 158.336 261.302 1.00 73.44 ATOM 172 NE2 GLN G 103 115.562 157.512 260.105 1.00 66.05 ATOM 173 C GLN G 103 114.998 152.933 261.817 1.00 64.43 ATOM 174 O GLN G 103 116.105 153.415 262.066 1.00 63.62 ATOM 175 N MET G 104 114.483 151.904 262.485 1.00 66.76 ATOM 176 CA MET G 104 115.216 151.195 263.530 1.00 69.28 ATOM 177 CB MET G 104 114.613 151.491 264.906 1.00 68.23 ATOM 178 CG MET G 104 114.654 152.950 265.317 1.00 68.71 ATOM 179 SD MET G 104 113.818 153.260 266.885 1.00 66.43 ATOM 180 CE MET G 104 114.822 152.291 268.004 1.00 66.60 ATOM 181 C MET G 104 115.159 149.694 263.263 1.00 72.27 ATOM 182 O MET G 104 114.953 148.899 264.182 1.00 75.09 ATOM 183 N HIS G 105 115.346 149.311 262.002 1.00 74.16 ATOM 184 CA HIS G 105 115.133 147.929 261.571 1.00 75.32 ATOM 185 CB HIS G 105 114.363 147.903 260.245 1.00 75.84 ATOM 186 CG HIS G 105 114.949 148.786 259.186 1.00 79.86 ATOM 187 ND1 HIS G 105 114.760 150.152 259.165 1.00 82.57 ATOM 188 CE1 HIS G 105 115.388 150.667 258.123 1.00 81.83 ATOM 189 NE2 HIS G 105 115.977 149.684 257.465 1.00 82.90 ATOM 190 CD2 HIS G 105 115.718 148.498 258.108 1.00 81.12 ATOM 191 C HIS G 105 116.416 147.098 261.459 1.00 74.95 ATOM 192 O HIS G 105 116.720 146.554 260.395 1.00 75.35 ATOM 193 N GLU G 106 117.157 146.993 262.558 1.00 73.86 ATOM 194 CA GLU G 106 118.354 146.154 262.592 1.00 73.60 ATOM 195 CB GLU G 106 119.459 146.809 263.423 1.00 73.44 ATOM 196 CG GLU G 106 120.031 148.068 262.795 1.00 77.59 ATOM 197 CD GLU G 106 121.423 148.396 263.301 1.00 84.35 ATOM 198 OE1 GLU G 106 121.950 149.470 262.939 1.00 84.85 ATOM 199 OE2 GLU G 106 121.994 147.580 264.056 1.00 85.31 ATOM 200 C GLU G 106 118.031 144.761 263.131 1.00 72.43 ATOM 201 O GLU G 106 117.067 144.587 263.879 1.00 71.55 ATOM 202 N ASP G 107 118.840 143.774 262.750 1.00 71.49 ATOM 203 CA ASP G 107 118.583 142.383 263.124 1.00 69.55 ATOM 204 CB ASP G 107 119.566 141.427 262.435 1.00 70.18 ATOM 205 CG ASP G 107 120.945 141.436 263.072 1.00 74.60 ATOM 206 OD1 ASP G 107 121.499 140.339 263.301 1.00 76.60 ATOM 207 OD2 ASP G 107 121.477 142.534 263.342 1.00 81.53 ATOM 208 C ASP G 107 118.587 142.167 264.637 1.00 67.04 ATOM 209 O ASP G 107 119.262 142.882 265.382 1.00 64.48 ATOM 210 N ILE G 108 117.822 141.174 265.077 1.00 64.93 ATOM 211 CA ILE G 108 117.628 140.904 266.498 1.00 62.77 ATOM 212 CB ILE G 108 116.635 139.731 266.711 1.00 63.98 ATOM 213 CG1 ILE G 108 116.309 139.552 268.196 1.00 62.43 ATOM 214 CD1 ILE G 108 115.309 138.458 268.473 1.00 61.90 ATOM 215 CG2 ILE G 108 117.174 138.442 266.101 1.00 60.69 ATOM 216 C ILE G 108 118.943 140.628 267.231 1.00 62.26 ATOM 217 O ILE G 108 119.063 140.894 268.428 1.00 59.70 ATOM 218 N CYS G 109 119.933 140.119 266.504 1.00 62.58 ATOM 219 CA CYS G 109 121.207 139.736 267.109 1.00 64.41 ATOM 220 CB CYS G 109 121.983 138.798 266.181 1.00 64.72 ATOM 221 SG CYS G 109 121.250 137.151 266.055 1.00 64.07 ATOM 222 C CYS G 109 122.078 140.920 267.529 1.00 64.56 ATOM 223 O CYS G 109 123.172 140.733 268.059 1.00 63.76 ATOM 224 N SER G 110 121.590 142.135 267.299 1.00 66.11 ATOM 225 CA SER G 110 122.316 143.330 267.712 1.00 66.89 ATOM 226 CB SER G 110 122.588 144.247 266.516 1.00 66.15 ATOM 227 OG SER G 110 121.385 144.603 265.861 1.00 72.90 ATOM 228 C SER G 110 121.579 144.082 268.820 1.00 67.46 ATOM 229 O SER G 110 122.080 145.075 269.346 1.00 68.06 ATOM 230 N LEU G 111 120.388 143.603 269.172 1.00 68.12 ATOM 231 CA LEU G 111 119.654 144.148 270.311 1.00 69.17 ATOM 232 CB LEU G 111 118.147 143.985 270.119 1.00 66.78 ATOM 233 CG LEU G 111 117.419 145.073 269.325 1.00 73.77 ATOM 234 CD1 LEU G 111 118.003 145.237 267.925 1.00 77.41 ATOM 235 CD2 LEU G 111 115.926 144.772 269.258 1.00 71.97 ATOM 236 C LEU G 111 120.095 143.453 271.592 1.00 67.96 ATOM 237 O LEU G 111 119.781 143.892 272.700 1.00 68.41 ATOM 238 N TRP G 112 120.831 142.361 271.425 1.00 66.65 ATOM 239 CA TRP G 112 121.335 141.592 272.551 1.00 64.42 ATOM 240 CB TRP G 112 120.645 140.231 272.610 1.00 61.87 ATOM 241 CG TRP G 112 119.156 140.323 272.677 1.00 62.17 ATOM 242 CD1 TRP G 112 118.294 140.473 271.629 1.00 63.44 ATOM 243 NE1 TRP G 112 117.000 140.516 272.084 1.00 63.84 ATOM 244 CE2 TRP G 112 117.007 140.393 273.449 1.00 63.19 ATOM 245 CD2 TRP G 112 118.348 140.269 273.856 1.00 60.75 ATOM 246 CE3 TRP G 112 118.630 140.125 275.218 1.00 72.16 ATOM 247 CZ3 TRP G 112 117.578 140.108 276.115 1.00 65.69 ATOM 248 CH2 TRP G 112 116.256 140.236 275.681 1.00 61.72 ATOM 249 CZ2 TRP G 112 115.950 140.380 274.355 1.00 69.33 ATOM 250 C TRP G 112 122.838 141.396 272.432 1.00 61.87 ATOM 251 O TRP G 112 123.351 141.087 271.355 1.00 60.14 ATOM 252 N ASP G 113 123.541 141.583 273.541 1.00 61.16 ATOM 253 CA ASP G 113 124.959 141.268 273.594 1.00 64.09 ATOM 254 CB ASP G 113 125.787 142.494 273.991 1.00 64.63 ATOM 255 CG ASP G 113 126.011 143.452 272.833 1.00 61.97 ATOM 256 OD1 ASP G 113 126.641 144.511 273.052 1.00 65.58 ATOM 257 OD2 ASP G 113 125.565 143.150 271.705 1.00 52.96 ATOM 258 C ASP G 113 125.189 140.128 274.576 1.00 64.69 ATOM 259 O ASP G 113 124.390 139.909 275.488 1.00 66.85 ATOM 260 N GLN G 114 126.280 139.399 274.379 1.00 63.87 ATOM 261 CA GLN G 114 126.615 138.290 275.254 1.00 62.92 ATOM 262 CB GLN G 114 127.618 137.373 274.566 1.00 60.17 ATOM 263 CG GLN G 114 127.846 136.065 275.279 1.00 56.64 ATOM 264 CD GLN G 114 128.680 135.112 274.460 1.00 47.89 ATOM 265 OE1 GLN G 114 128.731 135.212 273.233 1.00 42.15 ATOM 266 NE2 GLN G 114 129.340 134.180 275.131 1.00 41.41 ATOM 267 C GLN G 114 127.180 138.820 276.566 1.00 65.51 ATOM 268 O GLN G 114 128.151 139.577 276.570 1.00 68.10 ATOM 269 N SER G 115 126.564 138.428 277.677 1.00 67.68 ATOM 270 CA SER G 115 126.960 138.936 278.988 1.00 71.51 ATOM 271 CB SER G 115 125.806 138.821 279.987 1.00 71.90 ATOM 272 OG SER G 115 125.428 137.471 280.182 1.00 78.29 ATOM 273 C SER G 115 128.196 138.234 279.533 1.00 72.16 ATOM 274 O SER G 115 128.337 137.018 279.406 1.00 71.29 ATOM 275 N LEU G 116 129.088 139.012 280.139 1.00 76.15 ATOM 276 CA LEU G 116 130.311 138.478 280.733 1.00 79.24 ATOM 277 CB LEU G 116 131.518 139.356 280.385 1.00 78.18 ATOM 278 CG LEU G 116 131.990 139.429 278.928 1.00 78.20 ATOM 279 CD1 LEU G 116 132.078 138.040 278.311 1.00 79.00 ATOM 280 CD2 LEU G 116 131.090 140.336 278.097 1.00 83.72 ATOM 281 C LEU G 116 130.177 138.357 282.248 1.00 81.65 ATOM 282 O LEU G 116 131.126 137.975 282.934 1.00 82.87 ATOM 283 N LYS G 117 128.997 138.694 282.761 1.00 85.40 ATOM 284 CA LYS G 117 128.708 138.601 284.189 1.00 88.53 ATOM 285 CB LYS G 117 127.231 138.897 284.458 1.00 90.23 ATOM 286 CG LYS G 117 126.853 140.368 284.487 1.00 91.98 ATOM 287 CD LYS G 117 125.372 140.523 284.818 1.00 90.42 ATOM 288 CE LYS G 117 125.002 141.970 285.107 1.00 95.74 ATOM 289 NZ LYS G 117 125.112 142.839 283.903 1.00 93.61 ATOM 290 C LYS G 117 129.038 137.216 284.730 1.00 90.27 ATOM 291 O LYS G 117 128.485 136.219 284.262 1.00 89.49 ATOM 292 N PRO G 118 129.944 137.149 285.721 1.00 93.06 ATOM 293 CA PRO G 118 130.218 135.888 286.401 1.00 94.76 ATOM 294 CB PRO G 118 131.143 136.304 287.548 1.00 95.10 ATOM 295 CG PRO G 118 131.800 137.550 287.069 1.00 94.78 ATOM 296 CD PRO G 118 130.761 138.255 286.250 1.00 92.78 ATOM 297 C PRO G 118 128.922 135.307 286.952 1.00 96.74 ATOM 298 O PRO G 118 128.104 136.040 287.509 1.00 97.77 ATOM 299 N CYS G 119 128.734 134.002 286.787 1.00 98.23 ATOM 300 CA CYS G 119 127.484 133.356 287.173 1.00 99.23 ATOM 301 CB CYS G 119 127.484 131.891 286.740 1.00 98.98 ATOM 302 SG CYS G 119 125.871 131.089 286.850 1.00 99.30 ATOM 303 C CYS G 119 127.210 133.467 288.672 1.00 99.55 ATOM 304 O CYS G 119 126.065 133.648 289.088 1.00 100.52 ATOM 305 N VAL G 120 128.265 133.361 289.474 1.00 99.80 ATOM 306 CA VAL G 120 128.145 133.467 290.925 1.00 99.48 ATOM 307 CB VAL G 120 129.403 132.934 291.636 1.00 98.42 ATOM 308 CG1 VAL G 120 130.631 133.723 291.205 1.00 98.47 ATOM 309 CG2 VAL G 120 129.224 132.993 293.146 1.00 99.05 ATOM 310 C VAL G 120 127.896 134.909 291.360 1.00 99.64 ATOM 311 O VAL G 120 126.749 135.343 291.479 1.00 98.92 ATOM 312 N ALA G 204 123.781 125.256 288.215 1.00 66.51 ATOM 313 CA ALA G 204 122.640 126.133 287.988 1.00 68.31 ATOM 314 CB ALA G 204 122.091 126.635 289.316 1.00 68.15 ATOM 315 C ALA G 204 123.016 127.306 287.084 1.00 67.75 ATOM 316 O ALA G 204 122.442 128.391 287.188 1.00 67.37 ATOM 317 N CYS G 205 123.973 127.075 286.190 1.00 68.37 ATOM 318 CA CYS G 205 124.520 128.135 285.348 1.00 68.94 ATOM 319 CB CYS G 205 126.004 128.334 285.661 1.00 71.63 ATOM 320 SG CYS G 205 126.335 129.148 287.232 1.00 87.93 ATOM 321 C CYS G 205 124.368 127.847 283.861 1.00 64.42 ATOM 322 O CYS G 205 124.712 126.762 283.401 1.00 65.93 ATOM 323 N PRO G 206 123.849 128.823 283.100 1.00 60.57 ATOM 324 CA PRO G 206 123.858 128.716 281.647 1.00 57.00 ATOM 325 CB PRO G 206 122.867 129.802 281.203 1.00 56.42 ATOM 326 CG PRO G 206 122.221 130.322 282.466 1.00 58.29 ATOM 327 CD PRO G 206 123.205 130.064 283.552 1.00 60.21 ATOM 328 C PRO G 206 125.251 129.020 281.101 1.00 53.62 ATOM 329 O PRO G 206 125.940 129.898 281.621 1.00 55.05 ATOM 330 N LYS G 207 125.659 128.289 280.068 1.00 48.86 ATOM 331 CA LYS G 207 126.973 128.471 279.458 1.00 44.45 ATOM 332 CB LYS G 207 127.183 127.444 278.343 1.00 42.31 ATOM 333 CG LYS G 207 128.636 127.117 278.037 1.00 38.42 ATOM 334 CD LYS G 207 129.255 128.138 277.098 1.00 37.53 ATOM 335 CE LYS G 207 130.651 127.687 276.676 1.00 41.13 ATOM 336 NZ LYS G 207 130.583 126.476 275.702 1.00 34.09 ATOM 337 C LYS G 207 127.134 129.893 278.918 1.00 45.34 ATOM 338 O LYS G 207 128.158 130.536 279.140 1.00 41.12 ATOM 339 N VAL G 208 126.120 130.375 278.205 1.00 46.31 ATOM 340 CA VAL G 208 126.111 131.755 277.728 1.00 49.93 ATOM 341 CB VAL G 208 126.310 131.850 276.195 1.00 47.58 ATOM 342 CG1 VAL G 208 127.622 131.207 275.782 1.00 47.61 ATOM 343 CG2 VAL G 208 125.149 131.216 275.457 1.00 50.14 ATOM 344 C VAL G 208 124.812 132.453 278.126 1.00 54.24 ATOM 345 O VAL G 208 123.739 131.848 278.105 1.00 53.45 ATOM 346 N SER G 209 124.915 133.723 278.502 1.00 60.26 ATOM 347 CA SER G 209 123.737 134.499 278.885 1.00 65.15 ATOM 348 CB SER G 209 123.712 134.739 280.396 1.00 67.09 ATOM 349 OG SER G 209 123.189 133.610 281.077 1.00 75.37 ATOM 350 C SER G 209 123.666 135.821 278.132 1.00 65.25 ATOM 351 O SER G 209 124.688 136.373 277.726 1.00 65.26 ATOM 352 N PHE G 210 122.452 136.329 277.957 1.00 67.05 ATOM 353 CA PHE G 210 122.238 137.533 277.163 1.00 68.73 ATOM 354 CB PHE G 210 121.409 137.203 275.917 1.00 63.87 ATOM 355 CG PHE G 210 122.044 136.170 275.031 1.00 61.14 ATOM 356 CD1 PHE G 210 121.574 134.865 275.015 1.00 57.59 ATOM 357 CE1 PHE G 210 122.167 133.909 274.206 1.00 53.14 ATOM 358 CZ PHE G 210 123.241 134.251 273.406 1.00 54.76 ATOM 359 CE2 PHE G 210 123.723 135.550 273.418 1.00 50.73 ATOM 360 CD2 PHE G 210 123.128 136.497 274.230 1.00 54.12 ATOM 361 C PHE G 210 121.581 138.660 277.954 1.00 70.50 ATOM 362 O PHE G 210 120.653 138.430 278.734 1.00 73.45 ATOM 363 N GLU G 211 122.075 139.876 277.742 1.00 71.43 ATOM 364 CA GLU G 211 121.470 141.070 278.318 1.00 75.52 ATOM 365 CB GLU G 211 122.495 141.869 279.117 1.00 76.41 ATOM 366 CG GLU G 211 122.984 141.181 280.375 1.00 84.91 ATOM 367 CD GLU G 211 123.971 142.030 281.141 1.00 96.50 ATOM 368 OE1 GLU G 211 124.878 141.460 281.784 1.00 104.68 ATOM 369 OE2 GLU G 211 123.846 143.272 281.094 1.00 104.23 ATOM 370 C GLU G 211 120.897 141.950 277.216 1.00 77.39 ATOM 371 O GLU G 211 121.531 142.140 276.175 1.00 77.96 ATOM 372 N PRO G 212 119.691 142.493 277.441 1.00 77.79 ATOM 373 CA PRO G 212 119.100 143.414 276.480 1.00 78.66 ATOM 374 CB PRO G 212 117.627 143.447 276.893 1.00 77.09 ATOM 375 CG PRO G 212 117.640 143.163 278.352 1.00 78.65 ATOM 376 CD PRO G 212 118.826 142.273 278.615 1.00 75.46 ATOM 377 C PRO G 212 119.723 144.804 276.594 1.00 78.54 ATOM 378 O PRO G 212 119.965 145.292 277.702 1.00 81.91 ATOM 379 N ILE G 213 120.009 145.422 275.454 1.00 77.77 ATOM 380 CA ILE G 213 120.478 146.805 275.445 1.00 78.23 ATOM 381 CB ILE G 213 121.650 147.026 274.436 1.00 79.65 ATOM 382 CG1 ILE G 213 121.363 148.194 273.490 1.00 78.63 ATOM 383 CD1 ILE G 213 121.851 149.524 273.994 1.00 84.68 ATOM 384 CG2 ILE G 213 121.919 145.768 273.628 1.00 83.17 ATOM 385 C ILE G 213 119.296 147.744 275.197 1.00 74.38 ATOM 386 O ILE G 213 118.528 147.544 274.253 1.00 75.23 ATOM 387 N PRO G 214 119.131 148.756 276.070 1.00 71.20 ATOM 388 CA PRO G 214 117.985 149.659 276.010 1.00 68.23 ATOM 389 CB PRO G 214 118.384 150.792 276.955 1.00 66.04 ATOM 390 CG PRO G 214 119.297 150.156 277.933 1.00 70.17 ATOM 391 CD PRO G 214 120.049 149.100 277.172 1.00 70.89 ATOM 392 C PRO G 214 117.776 150.194 274.602 1.00 65.72 ATOM 393 O PRO G 214 118.737 150.602 273.953 1.00 64.13 ATOM 394 N ILE G 215 116.533 150.174 274.132 1.00 62.51 ATOM 395 CA ILE G 215 116.237 150.622 272.777 1.00 64.83 ATOM 396 CB ILE G 215 114.868 150.113 272.280 1.00 65.89 ATOM 397 CG1 ILE G 215 115.040 148.822 271.477 1.00 68.23 ATOM 398 CD1 ILE G 215 115.701 147.698 272.234 1.00 64.36 ATOM 399 CG2 ILE G 215 114.204 151.148 271.393 1.00 68.05 ATOM 400 C ILE G 215 116.324 152.138 272.664 1.00 64.33 ATOM 401 O ILE G 215 115.729 152.869 273.455 1.00 65.98 ATOM 402 N HIS G 216 117.091 152.600 271.684 1.00 60.87 ATOM 403 CA HIS G 216 117.275 154.020 271.458 1.00 60.52 ATOM 404 CB HIS G 216 118.335 154.581 272.407 1.00 58.62 ATOM 405 CG HIS G 216 119.667 153.908 272.291 1.00 57.51 ATOM 406 ND1 HIS G 216 120.704 154.435 271.554 1.00 57.61 ATOM 407 CE1 HIS G 216 121.752 153.634 271.635 1.00 60.11 ATOM 408 NE2 HIS G 216 121.429 152.602 272.394 1.00 63.56 ATOM 409 CD2 HIS G 216 120.131 152.750 272.819 1.00 54.48 ATOM 410 C HIS G 216 117.677 154.257 270.010 1.00 61.17 ATOM 411 O HIS G 216 118.071 153.329 269.306 1.00 59.77 ATOM 412 N TYR G 217 117.559 155.499 269.562 1.00 62.64 ATOM 413 CA TYR G 217 117.945 155.844 268.204 1.00 64.48 ATOM 414 CB TYR G 217 116.719 156.192 267.360 1.00 64.62 ATOM 415 CG TYR G 217 117.058 156.618 265.951 1.00 62.70 ATOM 416 CD1 TYR G 217 116.950 157.947 265.565 1.00 64.75 ATOM 417 CE1 TYR G 217 117.261 158.347 264.279 1.00 67.32 ATOM 418 CZ TYR G 217 117.691 157.412 263.361 1.00 70.13 ATOM 419 OH TYR G 217 118.002 157.811 262.081 1.00 69.74 ATOM 420 CE2 TYR G 217 117.810 156.083 263.721 1.00 66.37 ATOM 421 CD2 TYR G 217 117.496 155.695 265.010 1.00 59.16 ATOM 422 C TYR G 217 118.934 156.998 268.204 1.00 65.62 ATOM 423 O TYR G 217 118.722 158.012 268.867 1.00 65.39 ATOM 424 N CYS G 218 120.021 156.830 267.461 1.00 66.44 ATOM 425 CA CYS G 218 121.011 157.883 267.318 1.00 67.09 ATOM 426 CB CYS G 218 122.382 157.396 267.785 1.00 68.84 ATOM 427 SG CYS G 218 122.435 156.968 269.548 1.00 74.15 ATOM 428 C CYS G 218 121.058 158.374 265.876 1.00 66.10 ATOM 429 O CYS G 218 120.997 157.581 264.936 1.00 64.93 ATOM 430 N ALA G 219 121.150 159.690 265.712 1.00 66.09 ATOM 431 CA ALA G 219 121.139 160.306 264.392 1.00 67.01 ATOM 432 CB ALA G 219 120.874 161.800 264.508 1.00 66.28 ATOM 433 C ALA G 219 122.444 160.056 263.645 1.00 68.24 ATOM 434 O ALA G 219 123.526 160.285 264.187 1.00 69.43 ATOM 435 N PRO G 220 122.342 159.578 262.395 1.00 68.39 ATOM 436 CA PRO G 220 123.507 159.387 261.535 1.00 67.59 ATOM 437 CB PRO G 220 122.919 158.724 260.282 1.00 67.57 ATOM 438 CG PRO G 220 121.575 158.211 260.697 1.00 69.11 ATOM 439 CD PRO G 220 121.094 159.174 261.728 1.00 68.80 ATOM 440 C PRO G 220 124.141 160.726 261.171 1.00 66.64 ATOM 441 O PRO G 220 123.536 161.777 261.390 1.00 66.28 ATOM 442 N ALA G 221 125.351 160.684 260.621 1.00 65.75 ATOM 443 CA ALA G 221 126.062 161.899 260.234 1.00 63.48 ATOM 444 CB ALA G 221 127.421 161.554 259.646 1.00 63.93 ATOM 445 C ALA G 221 125.247 162.729 259.246 1.00 62.07 ATOM 446 O ALA G 221 124.604 162.187 258.347 1.00 61.63 ATOM 447 N GLY G 222 125.273 164.046 259.426 1.00 60.25 ATOM 448 CA GLY G 222 124.528 164.953 258.559 1.00 58.52 ATOM 449 C GLY G 222 123.089 165.145 258.998 1.00 57.07 ATOM 450 O GLY G 222 122.338 165.900 258.379 1.00 56.59 ATOM 451 N PHE G 223 122.704 164.459 260.071 1.00 56.64 ATOM 452 CA PHE G 223 121.346 164.547 260.602 1.00 55.52 ATOM 453 CB PHE G 223 120.561 163.267 260.292 1.00 57.30 ATOM 454 CG PHE G 223 120.408 162.984 258.824 1.00 58.90 ATOM 455 CD1 PHE G 223 121.237 162.068 258.191 1.00 60.08 ATOM 456 CE1 PHE G 223 121.099 161.802 256.840 1.00 60.76 ATOM 457 CZ PHE G 223 120.123 162.454 256.106 1.00 62.10 ATOM 458 CE2 PHE G 223 119.289 163.368 256.725 1.00 58.72 ATOM 459 CD2 PHE G 223 119.433 163.629 258.076 1.00 57.90 ATOM 460 C PHE G 223 121.346 164.794 262.110 1.00 53.60 ATOM 461 O PHE G 223 122.286 164.416 262.810 1.00 53.29 ATOM 462 N ALA G 224 120.286 165.427 262.602 1.00 52.19 ATOM 463 CA ALA G 224 120.118 165.652 264.034 1.00 51.71 ATOM 464 CB ALA G 224 120.424 167.099 264.386 1.00 51.41 ATOM 465 C ALA G 224 118.703 165.284 264.472 1.00 51.78 ATOM 466 O ALA G 224 117.780 165.262 263.657 1.00 54.51 ATOM 467 N ILE G 225 118.534 164.989 265.757 1.00 49.20 ATOM 468 CA ILE G 225 117.212 164.696 266.294 1.00 46.97 ATOM 469 CB ILE G 225 117.221 163.461 267.215 1.00 47.18 ATOM 470 CG1 ILE G 225 117.829 162.253 266.498 1.00 48.44 ATOM 471 CD1 ILE G 225 117.862 160.988 267.344 1.00 42.43 ATOM 472 CG2 ILE G 225 115.809 163.144 267.692 1.00 43.98 ATOM 473 C ILE G 225 116.664 165.889 267.072 1.00 48.18 ATOM 474 O ILE G 225 117.328 166.419 267.962 1.00 49.65 ATOM 475 N LEU G 226 115.453 166.310 266.724 1.00 48.03 ATOM 476 CA LEU G 226 114.773 167.371 267.450 1.00 47.15 ATOM 477 CB LEU G 226 113.924 168.204 266.495 1.00 46.71 ATOM 478 CG LEU G 226 114.633 168.782 265.271 1.00 46.15 ATOM 479 CD1 LEU G 226 113.631 169.481 264.372 1.00 42.30 ATOM 480 CD2 LEU G 226 115.736 169.739 265.692 1.00 50.92 ATOM 481 C LEU G 226 113.891 166.767 268.536 1.00 48.10 ATOM 482 O LEU G 226 113.097 165.868 268.269 1.00 47.13 ATOM 483 N LYS G 227 114.034 167.264 269.761 1.00 50.92 ATOM 484 CA LYS G 227 113.262 166.756 270.891 1.00 54.46 ATOM 485 CB LYS G 227 114.197 166.240 271.988 1.00 53.30 ATOM 486 CG LYS G 227 113.490 165.730 273.234 1.00 53.54 ATOM 487 CD LYS G 227 114.496 165.293 274.291 1.00 58.36 ATOM 488 CE LYS G 227 113.839 164.465 275.389 1.00 63.73 ATOM 489 NZ LYS G 227 112.840 165.249 276.168 1.00 65.72 ATOM 490 C LYS G 227 112.326 167.822 271.455 1.00 56.68 ATOM 491 O LYS G 227 112.773 168.849 271.966 1.00 55.79 ATOM 492 N CYS G 228 111.025 167.568 271.356 1.00 61.67 ATOM 493 CA CYS G 228 110.011 168.484 271.870 1.00 62.93 ATOM 494 CB CYS G 228 108.664 168.216 271.191 1.00 62.71 ATOM 495 SG CYS G 228 107.339 169.370 271.628 1.00 68.88 ATOM 496 C CYS G 228 109.881 168.349 273.387 1.00 63.75 ATOM 497 O CYS G 228 109.497 167.294 273.894 1.00 62.45 ATOM 498 N ASN G 229 110.206 169.422 274.104 1.00 64.92 ATOM 499 CA ASN G 229 110.158 169.418 275.566 1.00 65.65 ATOM 500 CB ASN G 229 111.394 170.106 276.152 1.00 65.50 ATOM 501 CG ASN G 229 112.614 169.206 276.162 1.00 64.22 ATOM 502 OD1 ASN G 229 112.530 168.022 275.842 1.00 62.00 ATOM 503 ND2 ASN G 229 113.758 169.767 276.537 1.00 65.96 ATOM 504 C ASN G 229 108.885 170.040 276.139 1.00 66.74 ATOM 505 O ASN G 229 108.943 170.925 276.994 1.00 67.43 ATOM 506 N ASN G 230 107.738 169.573 275.658 1.00 68.32 ATOM 507 CA ASN G 230 106.450 169.985 276.201 1.00 69.28 ATOM 508 CB ASN G 230 105.546 170.530 275.094 1.00 68.14 ATOM 509 CG ASN G 230 104.213 171.025 275.619 1.00 63.85 ATOM 510 OD1 ASN G 230 104.076 171.343 276.801 1.00 60.21 ATOM 511 ND2 ASN G 230 103.221 171.095 274.740 1.00 60.29 ATOM 512 C ASN G 230 105.778 168.814 276.915 1.00 71.31 ATOM 513 O ASN G 230 105.325 167.863 276.276 1.00 71.18 ATOM 514 N LYS G 231 105.723 168.893 278.242 1.00 73.45 ATOM 515 CA LYS G 231 105.208 167.806 279.077 1.00 75.01 ATOM 516 CB LYS G 231 105.060 168.274 280.528 1.00 74.99 ATOM 517 CG LYS G 231 106.360 168.777 281.142 1.00 73.86 ATOM 518 CD LYS G 231 106.142 169.355 282.530 1.00 71.29 ATOM 519 CE LYS G 231 107.437 169.910 283.102 1.00 69.12 ATOM 520 NZ LYS G 231 107.249 170.466 284.469 1.00 65.53 ATOM 521 C LYS G 231 103.890 167.225 278.560 1.00 76.63 ATOM 522 O LYS G 231 103.747 166.006 278.436 1.00 76.03 ATOM 523 N THR G 232 102.934 168.101 278.261 1.00 77.58 ATOM 524 CA THR G 232 101.656 167.678 277.693 1.00 78.14 ATOM 525 CB THR G 232 100.465 168.363 278.392 1.00 78.20 ATOM 526 OG1 THR G 232 100.658 169.783 278.388 1.00 77.71 ATOM 527 CG2 THR G 232 100.336 167.877 279.830 1.00 78.04 ATOM 528 C THR G 232 101.610 167.969 276.194 1.00 78.44 ATOM 529 O THR G 232 101.235 169.065 275.775 1.00 78.88 ATOM 530 N PHE G 233 101.997 166.980 275.395 1.00 78.48 ATOM 531 CA PHE G 233 102.069 167.133 273.946 1.00 79.07 ATOM 532 CB PHE G 233 103.507 167.443 273.523 1.00 79.52 ATOM 533 CG PHE G 233 103.715 167.484 272.036 1.00 81.37 ATOM 534 CD1 PHE G 233 102.978 168.346 271.239 1.00 83.16 ATOM 535 CE1 PHE G 233 103.175 168.387 269.869 1.00 84.04 ATOM 536 CZ PHE G 233 104.125 167.570 269.283 1.00 82.54 ATOM 537 CE2 PHE G 233 104.873 166.712 270.068 1.00 83.79 ATOM 538 CD2 PHE G 233 104.668 166.673 271.436 1.00 83.44 ATOM 539 C PHE G 233 101.559 165.873 273.253 1.00 79.37 ATOM 540 O PHE G 233 102.102 164.786 273.444 1.00 78.86 ATOM 541 N ASN G 234 100.515 166.031 272.444 1.00 80.48 ATOM 542 CA ASN G 234 99.834 164.897 271.819 1.00 81.41 ATOM 543 CB ASN G 234 98.502 165.345 271.203 1.00 82.95 ATOM 544 CG ASN G 234 98.683 166.361 270.087 1.00 90.59 ATOM 545 OD1 ASN G 234 99.373 166.099 269.104 1.00 91.56 ATOM 546 ND2 ASN G 234 98.059 167.527 270.236 1.00 103.25 ATOM 547 C ASN G 234 100.674 164.134 270.790 1.00 79.48 ATOM 548 O ASN G 234 100.285 163.056 270.339 1.00 79.33 ATOM 549 N GLY G 235 101.821 164.696 270.422 1.00 77.34 ATOM 550 CA GLY G 235 102.709 164.053 269.461 1.00 75.70 ATOM 551 C GLY G 235 102.771 164.777 268.130 1.00 74.85 ATOM 552 O GLY G 235 103.810 164.794 267.469 1.00 74.19 ATOM 553 N THR G 236 101.656 165.381 267.735 1.00 74.44 ATOM 554 CA THR G 236 101.590 166.098 266.468 1.00 74.48 ATOM 555 CB THR G 236 100.599 165.430 265.484 1.00 74.15 ATOM 556 OG1 THR G 236 100.545 166.183 264.266 1.00 74.70 ATOM 557 CG2 THR G 236 99.206 165.344 266.089 1.00 74.84 ATOM 558 C THR G 236 101.237 167.572 266.673 1.00 74.03 ATOM 559 O THR G 236 100.744 167.962 267.731 1.00 73.78 ATOM 560 N GLY G 237 101.504 168.387 265.657 1.00 73.90 ATOM 561 CA GLY G 237 101.267 169.823 265.742 1.00 73.51 ATOM 562 C GLY G 237 102.555 170.595 265.959 1.00 73.19 ATOM 563 O GLY G 237 103.644 170.047 265.791 1.00 73.69 ATOM 564 N PRO G 238 102.437 171.879 266.333 1.00 73.07 ATOM 565 CA PRO G 238 103.588 172.745 266.572 1.00 72.53 ATOM 566 CB PRO G 238 102.989 174.148 266.469 1.00 72.40 ATOM 567 CG PRO G 238 101.581 173.981 266.921 1.00 72.73 ATOM 568 CD PRO G 238 101.158 172.585 266.538 1.00 72.72 ATOM 569 C PRO G 238 104.216 172.540 267.952 1.00 72.02 ATOM 570 O PRO G 238 103.555 172.062 268.874 1.00 70.79 ATOM 571 N CYS G 239 105.488 172.908 268.078 1.00 72.47 ATOM 572 CA CYS G 239 106.220 172.771 269.333 1.00 72.91 ATOM 573 CB CYS G 239 106.878 171.392 269.418 1.00 73.09 ATOM 574 SG CYS G 239 107.954 171.150 270.854 1.00 73.09 ATOM 575 C CYS G 239 107.278 173.862 269.449 1.00 73.70 ATOM 576 O CYS G 239 108.150 173.982 268.588 1.00 74.70 ATOM 577 N THR G 240 107.198 174.653 270.515 1.00 74.31 ATOM 578 CA THR G 240 108.130 175.759 270.721 1.00 74.23 ATOM 579 CB THR G 240 107.462 176.940 271.456 1.00 73.95 ATOM 580 OG1 THR G 240 106.983 176.505 272.734 1.00 73.14 ATOM 581 CG2 THR G 240 106.299 177.485 270.642 1.00 74.64 ATOM 582 C THR G 240 109.376 175.322 271.489 1.00 74.57 ATOM 583 O THR G 240 110.501 175.553 271.044 1.00 75.18 ATOM 584 N ASN G 241 109.169 174.693 272.643 1.00 73.92 ATOM 585 CA ASN G 241 110.278 174.216 273.463 1.00 74.37 ATOM 586 CB ASN G 241 109.803 173.922 274.889 1.00 76.28 ATOM 587 CG ASN G 241 110.954 173.703 275.858 1.00 85.73 ATOM 588 OD1 ASN G 241 112.102 174.040 275.565 1.00 86.74 ATOM 589 ND2 ASN G 241 110.648 173.133 277.020 1.00 102.86 ATOM 590 C ASN G 241 110.941 172.985 272.845 1.00 72.43 ATOM 591 O ASN G 241 110.497 171.854 273.051 1.00 70.57 ATOM 592 N VAL G 242 112.004 173.219 272.081 1.00 70.29 ATOM 593 CA VAL G 242 112.706 172.154 271.371 1.00 67.80 ATOM 594 CB VAL G 242 112.654 172.379 269.841 1.00 67.75 ATOM 595 CG1 VAL G 242 113.262 171.198 269.099 1.00 68.42 ATOM 596 CG2 VAL G 242 111.222 172.616 269.384 1.00 68.06 ATOM 597 C VAL G 242 114.165 172.069 271.820 1.00 65.93 ATOM 598 O VAL G 242 114.683 172.994 272.444 1.00 66.45 ATOM 599 N SER G 243 114.818 170.954 271.507 1.00 63.53 ATOM 600 CA SER G 243 116.238 170.782 271.799 1.00 62.25 ATOM 601 CB SER G 243 116.443 170.286 273.232 1.00 61.66 ATOM 602 OG SER G 243 115.976 168.959 273.388 1.00 61.15 ATOM 603 C SER G 243 116.884 169.815 270.810 1.00 61.80 ATOM 604 O SER G 243 116.221 168.931 270.269 1.00 61.62 ATOM 605 N THR G 244 118.180 169.992 270.577 1.00 61.37 ATOM 606 CA THR G 244 118.920 169.131 269.664 1.00 61.05 ATOM 607 CB THR G 244 119.967 169.927 268.859 1.00 60.98 ATOM 608 OG1 THR G 244 119.335 171.035 268.208 1.00 63.76 ATOM 609 CG2 THR G 244 120.633 169.040 267.814 1.00 60.02 ATOM 610 C THR G 244 119.624 168.014 270.424 1.00 60.67 ATOM 611 O THR G 244 120.295 168.259 271.425 1.00 60.97 ATOM 612 N VAL G 245 119.455 166.787 269.947 1.00 61.53 ATOM 613 CA VAL G 245 120.155 165.632 270.504 1.00 62.51 ATOM 614 CB VAL G 245 119.253 164.804 271.450 1.00 62.49 ATOM 615 CG1 VAL G 245 119.118 165.490 272.804 1.00 66.08 ATOM 616 CG2 VAL G 245 117.888 164.561 270.820 1.00 58.72 ATOM 617 C VAL G 245 120.640 164.737 269.373 1.00 62.13 ATOM 618 O VAL G 245 120.181 164.858 268.237 1.00 62.67 ATOM 619 N GLN G 246 121.573 163.843 269.675 1.00 62.32 ATOM 620 CA GLN G 246 122.008 162.881 268.676 1.00 64.06 ATOM 621 CB GLN G 246 123.524 162.707 268.690 1.00 64.01 ATOM 622 CG GLN G 246 124.092 162.394 267.317 1.00 65.15 ATOM 623 CD GLN G 246 125.174 161.339 267.355 1.00 68.69 ATOM 624 OE1 GLN G 246 126.243 161.506 266.767 1.00 73.14 ATOM 625 NE2 GLN G 246 124.902 160.239 268.049 1.00 65.13 ATOM 626 C GLN G 246 121.319 161.541 268.892 1.00 65.40 ATOM 627 O GLN G 246 121.169 160.757 267.956 1.00 65.72 ATOM 628 N CYS G 247 120.896 161.287 270.128 1.00 67.14 ATOM 629 CA CYS G 247 120.229 160.033 270.473 1.00 66.90 ATOM 630 CB CYS G 247 121.169 159.121 271.269 1.00 67.79 ATOM 631 SG CYS G 247 122.751 158.756 270.464 1.00 73.76 ATOM 632 C CYS G 247 118.949 160.266 271.272 1.00 66.16 ATOM 633 O CYS G 247 118.839 161.236 272.022 1.00 66.23 ATOM 634 N THR G 248 117.984 159.366 271.102 1.00 65.97 ATOM 635 CA THR G 248 116.765 159.378 271.903 1.00 66.46 ATOM 636 CB THR G 248 115.604 158.676 271.177 1.00 65.81 ATOM 637 OG1 THR G 248 115.899 157.281 271.037 1.00 64.85 ATOM 638 CG2 THR G 248 115.386 159.285 269.801 1.00 64.08 ATOM 639 C THR G 248 117.029 158.654 273.216 1.00 67.08 ATOM 640 O THR G 248 118.071 158.020 273.377 1.00 68.23 ATOM 641 N HIS G 249 116.090 158.740 274.154 1.00 67.69 ATOM 642 CA HIS G 249 116.287 158.103 275.453 1.00 68.85 ATOM 643 CB HIS G 249 115.477 158.791 276.561 1.00 69.11 ATOM 644 CG HIS G 249 113.994 158.685 276.395 1.00 69.08 ATOM 645 ND1 HIS G 249 113.255 159.613 275.693 1.00 70.76 ATOM 646 CE1 HIS G 249 111.979 159.271 275.722 1.00 69.54 ATOM 647 NE2 HIS G 249 111.862 158.159 276.426 1.00 69.21 ATOM 648 CD2 HIS G 249 113.107 157.774 276.862 1.00 71.06 ATOM 649 C HIS G 249 116.014 156.607 275.405 1.00 68.83 ATOM 650 O HIS G 249 115.105 156.146 274.712 1.00 70.83 ATOM 651 N GLY G 250 116.827 155.856 276.141 1.00 70.45 ATOM 652 CA GLY G 250 116.751 154.403 276.145 1.00 70.60 ATOM 653 C GLY G 250 115.394 153.897 276.572 1.00 70.96 ATOM 654 O GLY G 250 114.796 154.408 277.520 1.00 69.81 ATOM 655 N ILE G 251 114.908 152.887 275.860 1.00 72.98 ATOM 656 CA ILE G 251 113.610 152.308 276.143 1.00 71.31 ATOM 657 CB ILE G 251 112.776 152.157 274.858 1.00 71.24 ATOM 658 CG1 ILE G 251 112.523 153.537 274.241 1.00 70.62 ATOM 659 CD1 ILE G 251 111.838 153.506 272.895 1.00 66.17 ATOM 660 CG2 ILE G 251 111.470 151.440 275.154 1.00 63.09 ATOM 661 C ILE G 251 113.787 150.960 276.825 1.00 73.60 ATOM 662 O ILE G 251 114.417 150.054 276.278 1.00 77.35 ATOM 663 N ARG G 252 113.241 150.852 278.032 1.00 73.90 ATOM 664 CA ARG G 252 113.316 149.631 278.823 1.00 75.73 ATOM 665 CB ARG G 252 114.425 149.758 279.870 1.00 72.25 ATOM 666 CG ARG G 252 114.666 148.512 280.707 1.00 71.94 ATOM 667 CD ARG G 252 115.668 148.794 281.825 1.00 80.61 ATOM 668 NE ARG G 252 116.025 147.612 282.614 1.00 89.29 ATOM 669 CZ ARG G 252 115.523 146.390 282.441 1.00 84.59 ATOM 670 NH1 ARG G 252 114.618 146.151 281.498 1.00 94.25 ATOM 671 NH2 ARG G 252 115.928 145.397 283.221 1.00 75.55 ATOM 672 C ARG G 252 111.966 149.395 279.498 1.00 72.88 ATOM 673 O ARG G 252 111.427 150.300 280.136 1.00 75.18 ATOM 674 N PRO G 253 111.415 148.177 279.373 1.00 69.69 ATOM 675 CA PRO G 253 111.990 147.007 278.719 1.00 70.13 ATOM 676 CB PRO G 253 111.200 145.856 279.344 1.00 69.15 ATOM 677 CG PRO G 253 109.851 146.435 279.572 1.00 65.34 ATOM 678 CD PRO G 253 110.083 147.886 279.936 1.00 68.98 ATOM 679 C PRO G 253 111.799 146.985 277.198 1.00 75.61 ATOM 680 O PRO G 253 110.859 147.615 276.651 1.00 70.73 ATOM 681 N VAL G 254 112.665 146.208 276.537 1.00 78.40 ATOM 682 CA VAL G 254 112.742 146.177 275.078 1.00 74.81 ATOM 683 CB VAL G 254 114.000 145.424 274.593 1.00 76.70 ATOM 684 CG1 VAL G 254 115.243 145.955 275.313 1.00 74.12 ATOM 685 CG2 VAL G 254 113.852 143.930 274.826 1.00 74.40 ATOM 686 C VAL G 254 111.505 145.609 274.408 1.00 72.39 ATOM 687 O VAL G 254 111.171 146.005 273.293 1.00 78.26 ATOM 688 N VAL G 255 110.830 144.670 275.068 1.00 70.76 ATOM 689 CA VAL G 255 109.535 144.208 274.583 1.00 64.86 ATOM 690 CB VAL G 255 109.553 142.735 274.058 1.00 70.61 ATOM 691 CG1 VAL G 255 110.969 142.284 273.740 1.00 68.68 ATOM 692 CG2 VAL G 255 108.900 141.783 275.054 1.00 71.78 ATOM 693 C VAL G 255 108.482 144.362 275.673 1.00 63.18 ATOM 694 O VAL G 255 108.765 144.168 276.857 1.00 58.75 ATOM 695 N SER G 256 107.268 144.713 275.256 1.00 62.98 ATOM 696 CA SER G 256 106.144 144.894 276.165 1.00 63.01 ATOM 697 CB SER G 256 106.332 146.163 276.992 1.00 64.83 ATOM 698 OG SER G 256 105.682 146.057 278.244 1.00 68.18 ATOM 699 C SER G 256 104.862 144.978 275.343 1.00 62.59 ATOM 700 O SER G 256 104.606 145.985 274.686 1.00 65.31 ATOM 701 N SER G 257 104.059 143.919 275.381 1.00 63.12 ATOM 702 CA SER G 257 102.954 143.771 274.436 1.00 61.14 ATOM 703 CB SER G 257 102.596 142.297 274.249 1.00 58.57 ATOM 704 OG SER G 257 102.082 141.743 275.445 1.00 63.69 ATOM 705 C SER G 257 101.699 144.576 274.776 1.00 62.37 ATOM 706 O SER G 257 101.016 145.067 273.877 1.00 63.31 ATOM 707 N GLN G 258 101.395 144.712 276.064 1.00 63.48 ATOM 708 CA GLN G 258 100.124 145.304 276.477 1.00 63.51 ATOM 709 CB GLN G 258 99.191 144.224 277.045 1.00 61.39 ATOM 710 CG GLN G 258 98.844 143.139 276.036 1.00 57.35 ATOM 711 CD GLN G 258 97.896 142.089 276.583 1.00 64.26 ATOM 712 OE1 GLN G 258 97.482 141.180 275.860 1.00 63.98 ATOM 713 NE2 GLN G 258 97.556 142.197 277.864 1.00 52.87 ATOM 714 C GLN G 258 100.293 146.465 277.457 1.00 63.13 ATOM 715 O GLN G 258 99.969 147.607 277.132 1.00 66.54 ATOM 716 N LEU G 259 100.790 146.173 278.655 1.00 64.50 ATOM 717 CA LEU G 259 101.102 147.216 279.625 1.00 62.73 ATOM 718 CB LEU G 259 101.174 146.636 281.041 1.00 61.59 ATOM 719 CG LEU G 259 99.983 145.790 281.505 1.00 65.68 ATOM 720 CD1 LEU G 259 100.313 145.071 282.800 1.00 59.41 ATOM 721 CD2 LEU G 259 98.724 146.635 281.662 1.00 63.12 ATOM 722 C LEU G 259 102.431 147.870 279.261 1.00 62.86 ATOM 723 O LEU G 259 103.266 147.257 278.592 1.00 58.83 ATOM 724 N LEU G 260 102.618 149.115 279.687 1.00 58.57 ATOM 725 CA LEU G 260 103.887 149.798 279.487 1.00 60.19 ATOM 726 CB LEU G 260 103.698 151.106 278.715 1.00 60.47 ATOM 727 CG LEU G 260 103.017 150.988 277.344 1.00 65.37 ATOM 728 CD1 LEU G 260 102.793 152.355 276.730 1.00 61.99 ATOM 729 CD2 LEU G 260 103.800 150.092 276.391 1.00 57.44 ATOM 730 C LEU G 260 104.522 150.050 280.846 1.00 62.67 ATOM 731 O LEU G 260 103.921 150.680 281.718 1.00 66.42 ATOM 732 N LEU G 261 105.739 149.546 281.024 1.00 61.06 ATOM 733 CA LEU G 261 106.385 149.566 282.328 1.00 60.15 ATOM 734 CB LEU G 261 106.782 148.144 282.747 1.00 56.20 ATOM 735 CG LEU G 261 105.801 147.004 282.456 1.00 64.47 ATOM 736 CD1 LEU G 261 106.471 145.662 282.682 1.00 70.33 ATOM 737 CD2 LEU G 261 104.531 147.115 283.291 1.00 63.64 ATOM 738 C LEU G 261 107.606 150.481 282.341 1.00 59.74 ATOM 739 O LEU G 261 108.256 150.676 281.316 1.00 59.86 ATOM 740 N ASN G 262 107.896 151.043 283.513 1.00 61.50 ATOM 741 CA ASN G 262 109.076 151.881 283.737 1.00 63.04 ATOM 742 CB ASN G 262 110.351 151.030 283.757 1.00 61.33 ATOM 743 CG ASN G 262 110.393 150.072 284.933 1.00 62.73 ATOM 744 OD1 ASN G 262 109.535 150.118 285.817 1.00 52.20 ATOM 745 ND2 ASN G 262 111.394 149.192 284.944 1.00 72.24 ATOM 746 C ASN G 262 109.235 153.055 282.770 1.00 66.01 ATOM 747 O ASN G 262 110.343 153.576 282.588 1.00 65.26 ATOM 748 N GLY G 263 108.127 153.479 282.169 1.00 65.97 ATOM 749 CA GLY G 263 108.142 154.614 281.254 1.00 69.91 ATOM 750 C GLY G 263 108.120 155.945 281.980 1.00 73.75 ATOM 751 O GLY G 263 108.310 156.006 283.196 1.00 74.95 ATOM 752 N SER G 264 107.895 157.019 281.232 1.00 76.06 ATOM 753 CA SER G 264 107.775 158.345 281.824 1.00 78.19 ATOM 754 CB SER G 264 108.355 159.409 280.887 1.00 79.01 ATOM 755 OG SER G 264 107.794 159.303 279.589 1.00 83.60 ATOM 756 C SER G 264 106.314 158.649 282.147 1.00 76.99 ATOM 757 O SER G 264 105.426 158.413 281.329 1.00 78.36 ATOM 758 N LEU G 265 106.076 159.169 283.346 1.00 76.66 ATOM 759 CA LEU G 265 104.726 159.480 283.805 1.00 74.89 ATOM 760 CB LEU G 265 104.671 159.474 285.335 1.00 75.76 ATOM 761 CG LEU G 265 104.925 158.130 286.019 1.00 75.43 ATOM 762 CD1 LEU G 265 105.065 158.309 287.522 1.00 73.86 ATOM 763 CD2 LEU G 265 103.812 157.146 285.690 1.00 64.91 ATOM 764 C LEU G 265 104.222 160.820 283.273 1.00 74.05 ATOM 765 O LEU G 265 105.006 161.727 282.987 1.00 72.78 ATOM 766 N ALA G 266 102.904 160.939 283.154 1.00 72.44 ATOM 767 CA ALA G 266 102.287 162.155 282.650 1.00 71.73 ATOM 768 CB ALA G 266 100.914 161.853 282.080 1.00 70.02 ATOM 769 C ALA G 266 102.195 163.218 283.740 1.00 72.63 ATOM 770 O ALA G 266 102.038 162.903 284.920 1.00 70.55 ATOM 771 N GLU G 267 102.298 164.479 283.333 1.00 74.95 ATOM 772 CA GLU G 267 102.252 165.597 284.269 1.00 77.46 ATOM 773 CB GLU G 267 102.946 166.820 283.667 1.00 76.59 ATOM 774 CG GLU G 267 103.404 167.850 284.686 1.00 80.50 ATOM 775 CD GLU G 267 104.720 167.478 285.353 1.00 83.53 ATOM 776 OE1 GLU G 267 105.158 166.315 285.220 1.00 88.36 ATOM 777 OE2 GLU G 267 105.317 168.354 286.012 1.00 78.13 ATOM 778 C GLU G 267 100.811 165.938 284.638 1.00 78.41 ATOM 779 O GLU G 267 100.052 166.441 283.808 1.00 80.22 ATOM 780 N GLU G 268 100.443 165.640 285.881 1.00 78.12 ATOM 781 CA GLU G 268 99.124 165.970 286.435 1.00 77.96 ATOM 782 CB GLU G 268 98.914 167.491 286.486 1.00 77.80 ATOM 783 CG GLU G 268 98.216 168.072 285.264 1.00 77.29 ATOM 784 CD GLU G 268 98.438 169.563 285.115 1.00 81.45 ATOM 785 OE1 GLU G 268 97.736 170.184 284.290 1.00 83.24 ATOM 786 OE2 GLU G 268 99.312 170.113 285.818 1.00 78.41 ATOM 787 C GLU G 268 97.924 165.292 285.760 1.00 77.40 ATOM 788 O GLU G 268 96.926 165.018 286.421 1.00 79.34 ATOM 789 N GLU G 269 98.015 165.023 284.458 1.00 76.51 ATOM 790 CA GLU G 269 96.877 164.482 283.708 1.00 75.94 ATOM 791 CB GLU G 269 96.415 166.486 282.647 1.00 76.39 ATOM 792 CG GLU G 269 95.461 166.564 283.151 1.00 84.29 ATOM 793 CD GLU G 269 94.000 166.157 283.048 1.00 88.65 ATOM 794 OE1 GLU G 269 93.694 164.961 283.241 1.00 94.35 ATOM 795 OE2 GLU G 269 93.154 167.035 282.774 1.00 88.83 ATOM 796 C GLU G 269 97.177 163.147 283.031 1.00 74.35 ATOM 797 O GLU G 269 98.259 162.955 282.481 1.00 77.37 ATOM 798 N VAL G 270 96.214 162.230 283.065 1.00 69.65 ATOM 799 CA VAL G 270 96.314 160.999 282.283 1.00 67.56 ATOM 800 CB VAL G 270 95.273 159.944 282.721 1.00 66.13 ATOM 801 CG1 VAL G 270 95.144 158.848 281.675 1.00 62.58 ATOM 802 CG2 VAL G 270 95.647 159.356 284.069 1.00 71.18 ATOM 803 C VAL G 270 96.107 161.339 280.812 1.00 65.12 ATOM 804 O VAL G 270 95.109 161.960 280.449 1.00 64.64 ATOM 805 N VAL G 271 97.055 160.943 279.970 1.00 62.75 ATOM 806 CA VAL G 271 97.035 161.329 278.566 1.00 62.22 ATOM 807 CB VAL G 271 98.294 162.146 278.191 1.00 62.29 ATOM 808 CG1 VAL G 271 98.231 162.599 276.741 1.00 66.30 ATOM 809 CG2 VAL G 271 98.439 163.351 279.108 1.00 61.88 ATOM 810 C VAL G 271 96.923 160.119 277.647 1.00 61.73 ATOM 811 O VAL G 271 97.627 159.123 277.824 1.00 66.54 ATOM 812 N ILE G 272 96.022 160.203 276.675 1.00 59.50 ATOM 813 CA ILE G 272 95.922 159.188 275.634 1.00 62.42 ATOM 814 CB ILE G 272 94.527 158.497 275.591 1.00 64.14 ATOM 815 CG1 ILE G 272 93.458 159.421 274.990 1.00 63.52 ATOM 816 CD1 ILE G 272 92.988 160.514 275.911 1.00 76.99 ATOM 817 CG2 ILE G 272 94.126 157.989 276.971 1.00 65.54 ATOM 818 C ILE G 272 96.230 159.821 274.287 1.00 59.19 ATOM 819 O ILE G 272 95.909 160.980 274.052 1.00 58.64 ATOM 820 N ARG G 273 96.877 159.068 273.407 1.00 59.18 ATOM 821 CA ARG G 273 97.149 159.575 272.073 1.00 59.00 ATOM 822 CB ARG G 273 98.491 160.314 272.011 1.00 58.67 ATOM 823 CG ARG G 273 99.702 159.499 272.405 1.00 60.18 ATOM 824 CD ARG G 273 100.962 160.367 272.414 1.00 68.09 ATOM 825 NE ARG G 273 100.904 161.422 273.425 1.00 73.14 ATOM 826 CZ ARG G 273 101.362 161.292 274.667 1.00 75.56 ATOM 827 NH1 ARG G 273 101.920 160.153 275.057 1.00 82.28 ATOM 828 NH2 ARG G 273 101.265 162.301 275.520 1.00 74.32 ATOM 829 C ARG G 273 97.071 158.497 271.010 1.00 58.30 ATOM 830 O ARG G 273 97.218 157.305 271.287 1.00 56.05 ATOM 831 N SER G 274 96.815 158.942 269.788 1.00 59.78 ATOM 832 CA SER G 274 96.717 158.064 268.641 1.00 59.96 ATOM 833 CB SER G 274 95.314 157.464 268.537 1.00 57.92 ATOM 834 OG SER G 274 95.108 156.885 267.263 1.00 56.28 ATOM 835 C SER G 274 97.012 158.888 267.409 1.00 62.13 ATOM 836 O SER G 274 96.902 160.114 267.430 1.00 64.20 ATOM 837 N CYS G 275 97.395 158.215 266.335 1.00 64.50 ATOM 838 CA CYS G 275 97.619 158.894 265.072 1.00 66.84 ATOM 839 CB CYS G 275 98.375 157.978 264.118 1.00 67.60 ATOM 840 SG CYS G 275 100.142 158.173 264.295 1.00 76.42 ATOM 841 C CYS G 275 96.300 159.348 264.466 1.00 66.46 ATOM 842 O CYS G 275 96.242 160.353 263.758 1.00 67.80 ATOM 843 N ASN G 276 95.245 158.597 264.765 1.00 64.81 ATOM 844 CA ASN G 276 93.902 158.893 264.290 1.00 65.04 ATOM 845 CB ASN G 276 93.774 158.521 262.812 1.00 64.91 ATOM 846 CG ASN G 276 92.451 158.952 262.205 1.00 65.52 ATOM 847 OD1 ASN G 276 91.663 159.663 262.829 1.00 65.59 ATOM 848 ND2 ASN G 276 92.202 158.513 260.973 1.00 67.21 ATOM 849 C ASN G 276 92.903 158.108 265.131 1.00 65.22 ATOM 850 O ASN G 276 92.720 156.907 264.929 1.00 64.80 ATOM 851 N PHE G 277 92.275 158.790 266.086 1.00 64.66 ATOM 852 CA PHE G 277 91.345 158.151 267.012 1.00 64.41 ATOM 853 CB PHE G 277 90.865 159.148 268.070 1.00 61.11 ATOM 854 CG PHE G 277 91.822 159.327 269.216 1.00 63.45 ATOM 855 CD1 PHE G 277 92.581 160.484 269.332 1.00 62.79 ATOM 856 CE1 PHE G 277 93.464 160.649 270.389 1.00 58.06 ATOM 857 CZ PHE G 277 93.594 159.650 271.342 1.00 60.54 ATOM 858 CE2 PHE G 277 92.840 158.493 271.236 1.00 54.62 ATOM 859 CD2 PHE G 277 91.963 158.336 270.180 1.00 50.15 ATOM 860 C PHE G 277 90.148 157.526 266.298 1.00 65.84 ATOM 861 O PHE G 277 89.617 156.504 266.738 1.00 65.98 ATOM 862 N THR G 278 89.739 158.142 265.192 1.00 64.48 ATOM 863 CA THR G 278 88.578 157.686 264.433 1.00 64.28 ATOM 864 CB THR G 278 88.080 158.784 263.474 1.00 62.37 ATOM 865 OG1 THR G 278 88.058 160.037 264.164 1.00 65.88 ATOM 866 CG2 THR G 278 86.677 158.468 262.965 1.00 65.71 ATOM 867 C THR G 278 88.898 156.430 263.634 1.00 63.71 ATOM 868 O THR G 278 88.002 155.685 263.238 1.00 64.92 ATOM 869 N ASP G 279 90.185 156.208 263.395 1.00 63.03 ATOM 870 CA ASP G 279 90.646 155.016 262.700 1.00 64.26 ATOM 871 CB ASP G 279 91.883 155.346 261.864 1.00 65.09 ATOM 872 CG ASP G 279 92.388 154.165 261.068 1.00 68.06 ATOM 873 OD1 ASP G 279 93.406 154.327 260.364 1.00 79.46 ATOM 874 OD2 ASP G 279 91.778 153.077 261.144 1.00 74.48 ATOM 875 C ASP G 279 90.965 153.929 263.720 1.00 63.33 ATOM 876 O ASP G 279 91.957 154.017 264.448 1.00 65.42 ATOM 877 N ASN G 280 90.123 152.902 263.778 1.00 61.93 ATOM 878 CA ASN G 280 90.290 151.860 264.787 1.00 64.94 ATOM 879 CB ASN G 280 89.042 150.977 264.880 1.00 66.63 ATOM 880 CG ASN G 280 88.802 150.176 263.628 1.00 69.26 ATOM 881 OD1 ASN G 280 89.035 150.650 262.518 1.00 85.89 ATOM 882 ND2 ASN G 280 88.332 148.952 263.796 1.00 79.95 ATOM 883 C ASN G 280 91.546 151.019 264.563 1.00 63.57 ATOM 884 O ASN G 280 91.982 150.295 265.456 1.00 66.01 ATOM 885 N ALA G 281 92.134 151.146 263.377 1.00 63.20 ATOM 886 CA ALA G 281 93.365 150.443 263.030 1.00 62.10 ATOM 887 CB ALA G 281 93.608 150.519 261.525 1.00 62.46 ATOM 888 C ALA G 281 94.584 150.973 263.790 1.00 62.55 ATOM 889 O ALA G 281 95.536 150.232 264.023 1.00 65.86 ATOM 890 N LYS G 282 94.557 152.251 264.165 1.00 61.64 ATOM 891 CA LYS G 282 95.670 152.858 264.903 1.00 59.45 ATOM 892 CB LYS G 282 95.699 154.379 264.714 1.00 61.05 ATOM 893 CG LYS G 282 95.466 154.854 263.290 1.00 62.18 ATOM 894 CD LYS G 282 96.460 154.252 262.314 1.00 62.88 ATOM 895 CE LYS G 282 97.862 154.770 262.553 1.00 76.24 ATOM 896 NZ LYS G 282 98.817 154.252 261.537 1.00 82.08 ATOM 897 C LYS G 282 95.615 152.530 266.395 1.00 61.19 ATOM 898 O LYS G 282 94.537 152.486 266.999 1.00 62.18 ATOM 899 N THR G 283 96.788 152.308 266.980 1.00 59.56 ATOM 900 CA THR G 283 96.910 151.985 268.391 1.00 58.45 ATOM 901 CB THR G 283 98.313 151.430 268.696 1.00 62.74 ATOM 902 OG1 THR G 283 98.534 150.265 267.899 1.00 61.87 ATOM 903 CG2 THR G 283 98.464 151.067 270.176 1.00 54.99 ATOM 904 C THR G 283 96.671 153.217 269.256 1.00 59.47 ATOM 905 O THR G 283 97.082 154.324 268.905 1.00 59.20 ATOM 906 N ILE G 284 95.989 153.021 270.379 1.00 56.50 ATOM 907 CA ILE G 284 95.826 154.077 271.364 1.00 57.53 ATOM 908 CB ILE G 284 94.419 154.061 271.991 1.00 58.11 ATOM 909 CG1 ILE G 284 93.355 154.328 270.926 1.00 55.57 ATOM 910 CD1 ILE G 284 91.949 154.042 271.393 1.00 55.58 ATOM 911 CG2 ILE G 284 94.321 155.083 273.115 1.00 54.96 ATOM 912 C ILE G 284 96.864 153.865 272.457 1.00 59.26 ATOM 913 O ILE G 284 96.928 152.802 273.067 1.00 58.20 ATOM 914 N ILE G 285 97.684 154.880 272.687 1.00 58.43 ATOM 915 CA ILE G 285 98.734 154.801 273.686 1.00 60.58 ATOM 916 CB ILE G 285 100.077 155.293 273.114 1.00 62.14 ATOM 917 CG1 ILE G 285 100.485 154.425 271.914 1.00 63.44 ATOM 918 CD1 ILE G 285 101.736 154.900 271.191 1.00 62.39 ATOM 919 CG2 ILE G 285 101.155 155.304 274.196 1.00 55.13 ATOM 920 C ILE G 285 98.339 155.631 274.900 1.00 61.16 ATOM 921 O ILE G 285 98.127 156.843 274.799 1.00 59.78 ATOM 922 N VAL G 286 98.220 154.961 276.043 1.00 61.66 ATOM 923 CA VAL G 286 97.830 155.616 277.284 1.00 60.22 ATOM 924 CB VAL G 286 96.844 154.755 278.093 1.00 60.79 ATOM 925 CG1 VAL G 286 96.336 155.524 279.301 1.00 57.91 ATOM 926 CG2 VAL G 286 95.687 154.320 277.222 1.00 60.23 ATOM 927 C VAL G 286 99.051 155.884 278.141 1.00 60.26 ATOM 928 O VAL G 286 99.932 155.037 278.260 1.00 64.83 ATOM 929 N GLN G 287 99.099 157.072 278.731 1.00 60.06 ATOM 930 CA GLN G 287 100.169 157.438 279.644 1.00 59.25 ATOM 931 CB GLN G 287 101.003 158.571 279.047 1.00 56.49 ATOM 932 CG GLN G 287 102.213 158.972 279.874 1.00 63.03 ATOM 933 CD GLN G 287 102.857 160.248 279.368 1.00 63.69 ATOM 934 OE1 GLN G 287 102.168 161.185 278.967 1.00 70.48 ATOM 935 NE2 GLN G 287 104.182 160.292 279.389 1.00 71.79 ATOM 936 C GLN G 287 99.554 157.867 280.969 1.00 59.66 ATOM 937 O GLN G 287 98.795 158.833 281.025 1.00 59.93 ATOM 938 N LEU G 288 99.874 157.141 282.035 1.00 63.14 ATOM 939 CA LEU G 288 99.283 157.412 283.344 1.00 62.80 ATOM 940 CB LEU G 288 99.306 156.154 284.213 1.00 64.44 ATOM 941 CG LEU G 288 98.864 154.842 283.562 1.00 57.79 ATOM 942 CD1 LEU G 288 99.084 153.687 284.529 1.00 58.62 ATOM 943 CD2 LEU G 288 97.411 154.911 283.111 1.00 51.81 ATOM 944 C LEU G 288 100.007 158.536 284.062 1.00 63.42 ATOM 945 O LEU G 288 101.103 158.930 283.668 1.00 64.42 ATOM 946 N ASN G 289 99.386 159.054 285.117 1.00 65.48 ATOM 947 CA ASN G 289 100.019 160.072 285.947 1.00 65.72 ATOM 948 CB ASN G 289 99.158 161.347 286.032 1.00 65.47 ATOM 949 CG ASN G 289 97.901 161.169 286.879 1.00 68.07 ATOM 950 OD1 ASN G 289 97.381 160.064 287.026 1.00 66.87 ATOM 951 ND2 ASN G 289 97.408 162.277 287.439 1.00 80.63 ATOM 952 C ASN G 289 100.362 159.528 287.332 1.00 66.75 ATOM 953 O ASN G 289 101.114 160.144 288.086 1.00 67.09 ATOM 954 N THR G 290 99.804 158.363 287.649 1.00 67.42 ATOM 955 CA THR G 290 100.091 157.667 288.896 1.00 69.47 ATOM 956 CB THR G 290 98.857 157.613 289.819 1.00 69.10 ATOM 957 OG1 THR G 290 98.285 158.921 289.942 1.00 75.23 ATOM 958 CG2 THR G 290 99.243 157.100 291.202 1.00 72.35 ATOM 959 C THR G 290 100.522 156.241 288.575 1.00 70.06 ATOM 960 O THR G 290 99.753 155.471 287.998 1.00 72.45 ATOM 961 N SER G 291 101.751 155.894 288.943 1.00 70.53 ATOM 962 CA SER G 291 102.294 154.577 288.623 1.00 71.20 ATOM 963 CB SER G 291 103.814 154.562 288.796 1.00 68.00 ATOM 964 OG SER G 291 104.168 154.748 290.152 1.00 75.84 ATOM 965 C SER G 291 101.660 153.473 289.464 1.00 68.55 ATOM 966 O SER G 291 101.422 153.642 290.658 1.00 71.13 ATOM 967 N VAL G 292 101.381 152.346 288.821 1.00 68.96 ATOM 968 CA VAL G 292 100.869 151.167 289.502 1.00 67.01 ATOM 969 CB VAL G 292 99.618 150.602 288.793 1.00 67.46 ATOM 970 CG1 VAL G 292 99.036 149.433 289.573 1.00 61.83 ATOM 971 CG2 VAL G 292 98.575 151.695 288.605 1.00 66.50 ATOM 972 C VAL G 292 101.968 150.114 289.502 1.00 67.10 ATOM 973 O VAL G 292 102.498 149.766 288.450 1.00 64.19 ATOM 974 N GLU G 293 102.333 149.625 290.682 1.00 69.44 ATOM 975 CA GLU G 293 103.395 148.631 290.767 1.00 70.15 ATOM 976 CB GLU G 293 104.007 148.571 292.176 1.00 70.88 ATOM 977 CG GLU G 293 103.033 148.823 293.319 1.00 78.90 ATOM 978 CD GLU G 293 102.893 150.299 293.655 1.00 89.03 ATOM 979 OE1 GLU G 293 101.745 150.771 293.799 1.00 92.46 ATOM 980 OE2 GLU G 293 103.931 150.988 293.769 1.00 88.95 ATOM 981 C GLU G 293 102.927 147.249 290.308 1.00 67.97 ATOM 982 O GLU G 293 101.765 146.876 290.481 1.00 65.92 ATOM 983 N ILE G 294 103.844 146.505 289.703 1.00 66.36 ATOM 984 CA ILE G 294 103.587 145.130 289.312 1.00 64.48 ATOM 985 CB ILE G 294 103.299 145.013 287.795 1.00 64.46 ATOM 986 CG1 ILE G 294 103.046 143.556 287.403 1.00 65.23 ATOM 987 CD1 ILE G 294 102.696 143.370 285.940 1.00 66.11 ATOM 988 CG2 ILE G 294 104.434 145.612 286.974 1.00 62.32 ATOM 989 C ILE G 294 104.770 144.252 289.723 1.00 64.50 ATOM 990 O ILE G 294 105.844 144.317 289.126 1.00 64.60 ATOM 991 N ASN G 295 104.572 143.448 290.764 1.00 65.32 ATOM 992 CA ASN G 295 105.627 142.574 291.270 1.00 66.57 ATOM 993 CB ASN G 295 105.639 142.562 292.801 1.00 68.21 ATOM 994 CG ASN G 295 105.510 143.947 293.399 1.00 71.05 ATOM 995 OD1 ASN G 295 106.020 144.927 292.853 1.00 67.90 ATOM 996 ND2 ASN G 295 104.823 144.035 294.532 1.00 81.53 ATOM 997 C ASN G 295 105.468 141.150 290.760 1.00 66.64 ATOM 998 O ASN G 295 104.467 140.496 291.040 1.00 67.37 ATOM 999 N CYS G 296 106.463 140.671 290.020 1.00 67.38 ATOM 1000 CA CYS G 296 106.431 139.316 289.481 1.00 68.49 ATOM 1001 CB CYS G 296 106.575 139.344 287.962 1.00 66.41 ATOM 1002 SG CYS G 296 105.418 140.468 287.158 1.00 68.65 ATOM 1003 C CYS G 296 107.522 138.451 290.103 1.00 70.21 ATOM 1004 O CYS G 296 108.619 138.930 290.394 1.00 69.94 ATOM 1005 N THR G 297 107.210 137.176 290.311 1.00 71.56 ATOM 1006 CA THR G 297 108.152 136.250 290.934 1.00 73.69 ATOM 1007 CB THR G 297 107.693 135.827 292.350 1.00 73.63 ATOM 1008 OG1 THR G 297 106.356 135.313 292.290 1.00 74.47 ATOM 1009 CG2 THR G 297 107.732 137.015 293.305 1.00 75.37 ATOM 1010 C THR G 297 108.373 135.008 290.074 1.00 71.87 ATOM 1011 O THR G 297 107.771 134.861 289.012 1.00 69.00 ATOM 1012 N GLY G 298 109.244 134.120 290.543 1.00 72.28 ATOM 1013 CA GLY G 298 109.565 132.900 289.813 1.00 70.53 ATOM 1014 C GLY G 298 108.447 131.880 289.858 1.00 68.38 ATOM 1015 O GLY G 298 108.277 131.097 288.924 1.00 65.76 ATOM 1016 N ALA G 299 107.681 131.896 290.947 1.00 67.84 ATOM 1017 CA ALA G 299 106.575 130.959 291.141 1.00 68.96 ATOM 1018 CB ALA G 299 105.969 131.130 292.531 1.00 67.84 ATOM 1019 C ALA G 299 105.499 131.091 290.060 1.00 70.06 ATOM 1020 O ALA G 299 104.507 130.359 290.066 1.00 70.85 ATOM 1021 N GLY G 329 105.700 132.033 289.142 1.00 69.44 ATOM 1022 CA GLY G 329 104.851 132.162 287.965 1.00 68.34 ATOM 1023 C GLY G 329 103.615 133.018 288.156 1.00 69.17 ATOM 1024 O GLY G 329 102.517 132.627 287.763 1.00 68.38 ATOM 1025 N HIS G 330 103.787 134.194 288.751 1.00 68.57 ATOM 1026 CA HIS G 330 102.665 135.111 288.924 1.00 67.94 ATOM 1027 CB HIS G 330 101.751 134.646 290.063 1.00 68.71 ATOM 1028 CG HIS G 330 102.425 134.591 291.399 1.00 68.31 ATOM 1029 ND1 HIS G 330 102.335 135.611 292.322 1.00 68.38 ATOM 1030 CE1 HIS G 330 103.024 135.288 293.402 1.00 74.28 ATOM 1031 NE2 HIS G 330 103.559 134.095 293.213 1.00 74.09 ATOM 1032 CD2 HIS G 330 103.200 133.637 291.969 1.00 69.02 ATOM 1033 C HIS G 330 103.094 136.560 289.143 1.00 67.55 ATOM 1034 O HIS G 330 104.147 136.833 289.724 1.00 68.20 ATOM 1035 N CYS G 331 102.268 137.483 288.661 1.00 66.25 ATOM 1036 CA CYS G 331 102.469 138.902 288.909 1.00 66.73 ATOM 1037 CB CYS G 331 102.509 139.685 287.596 1.00 64.84 ATOM 1038 SG CYS G 331 103.903 139.261 286.531 1.00 72.18 ATOM 1039 C CYS G 331 101.344 139.420 289.789 1.00 65.46 ATOM 1040 O CYS G 331 100.197 138.996 289.651 1.00 69.16 ATOM 1041 N ASN G 332 101.676 140.333 290.695 1.00 62.06 ATOM 1042 CA ASN G 332 100.687 140.909 291.596 1.00 59.94 ATOM 1043 CB ASN G 332 101.072 140.652 293.054 1.00 59.18 ATOM 1044 CG ASN G 332 100.902 139.201 293.455 1.00 58.21 ATOM 1045 OD1 ASN G 332 101.399 138.777 294.494 1.00 58.93 ATOM 1046 ND2 ASN G 332 100.198 138.431 292.631 1.00 58.37 ATOM 1047 C ASN G 332 100.486 142.401 291.365 1.00 60.05 ATOM 1048 O ASN G 332 101.449 143.147 291.190 1.00 59.85 ATOM 1049 N ILE G 333 99.224 142.820 291.358 1.00 59.96 ATOM 1050 CA ILE G 333 98.857 144.225 291.216 1.00 59.96 ATOM 1051 CB ILE G 333 98.391 144.535 289.777 1.00 62.29 ATOM 1052 CG1 ILE G 333 99.485 144.172 288.769 1.00 63.00 ATOM 1053 CD1 ILE G 333 99.010 144.109 287.347 1.00 66.71 ATOM 1054 CG2 ILE G 333 98.000 146.000 289.637 1.00 61.68 ATOM 1055 C ILE G 333 97.723 144.542 292.188 1.00 60.24 ATOM 1056 O ILE G 333 96.776 143.767 292.313 1.00 63.25 ATOM 1057 N ALA G 334 97.815 145.672 292.882 1.00 58.68 ATOM 1058 CA ALA G 334 96.762 146.069 293.814 1.00 59.78 ATOM 1059 CB ALA G 334 97.180 147.299 294.610 1.00 57.18 ATOM 1060 C ALA G 334 95.454 146.323 293.067 1.00 59.75 ATOM 1061 O ALA G 334 95.425 147.077 292.093 1.00 58.67 ATOM 1062 N ARG G 335 94.280 145.684 293.523 1.00 61.10 ATOM 1063 CA ARG G 335 93.087 145.768 292.844 1.00 62.80 ATOM 1064 CB ARG G 335 92.098 144.746 293.414 1.00 63.44 ATOM 1065 CG ARG G 335 90.792 144.657 292.629 1.00 63.16 ATOM 1066 CD ARG G 335 89.880 143.566 293.167 1.00 63.31 ATOM 1067 NE ARG G 335 90.510 142.251 293.096 1.00 61.03 ATOM 1068 CZ ARG G 335 90.421 141.434 292.052 1.00 64.01 ATOM 1069 NH1 ARG G 335 89.723 141.791 290.983 1.00 65.67 ATOM 1070 NH2 ARG G 335 91.032 140.259 292.079 1.00 69.24 ATOM 1071 C ARG G 335 92.490 147.168 292.914 1.00 62.12 ATOM 1072 O ARG G 335 91.884 147.636 291.955 1.00 66.45 ATOM 1073 N ALA G 336 92.664 147.830 294.051 1.00 61.69 ATOM 1074 CA ALA G 336 92.149 149.182 294.236 1.00 61.61 ATOM 1075 CB ALA G 336 92.321 149.623 295.686 1.00 58.98 ATOM 1076 C ALA G 336 92.825 150.174 293.290 1.00 60.70 ATOM 1077 O ALA G 336 92.171 151.053 292.729 1.00 61.88 ATOM 1078 N LYS G 337 94.134 150.024 293.115 1.00 59.07 ATOM 1079 CA LYS G 337 94.903 150.930 292.270 1.00 57.17 ATOM 1080 CB LYS G 337 96.397 150.820 292.584 1.00 56.58 ATOM 1081 CG LYS G 337 96.778 151.430 293.925 1.00 56.52 ATOM 1082 CD LYS G 337 98.086 150.863 294.452 1.00 64.52 ATOM 1083 CE LYS G 337 98.285 151.214 295.921 1.00 64.94 ATOM 1084 NZ LYS G 337 99.373 150.413 296.550 1.00 68.63 ATOM 1085 C LYS G 337 94.635 150.676 290.789 1.00 57.99 ATOM 1086 O LYS G 337 94.544 151.612 289.996 1.00 58.57 ATOM 1087 N TRP G 338 94.498 149.410 290.414 1.00 55.98 ATOM 1088 CA TRP G 338 94.145 149.099 289.039 1.00 57.47 ATOM 1089 CB TRP G 338 94.273 147.606 288.743 1.00 54.86 ATOM 1090 CG TRP G 338 94.035 147.307 287.291 1.00 63.02 ATOM 1091 CD1 TRP G 338 92.972 146.645 286.749 1.00 53.68 ATOM 1092 NE1 TRP G 338 93.101 146.584 285.381 1.00 63.74 ATOM 1093 CE2 TRP G 338 94.256 147.223 285.015 1.00 59.30 ATOM 1094 CD2 TRP G 338 94.869 147.694 286.192 1.00 59.96 ATOM 1095 CE3 TRP G 338 96.080 148.388 286.091 1.00 62.63 ATOM 1096 CZ3 TRP G 338 96.626 148.587 284.838 1.00 55.98 ATOM 1097 CH2 TRP G 338 95.993 148.107 283.689 1.00 54.13 ATOM 1098 CZ2 TRP G 338 94.810 147.426 283.755 1.00 58.75 ATOM 1099 C TRP G 338 92.734 149.602 288.733 1.00 56.87 ATOM 1100 O TRP G 338 92.489 150.179 287.678 1.00 55.53 ATOM 1101 N ASN G 339 91.816 149.393 289.671 1.00 59.21 ATOM 1102 CA ASN G 339 90.444 149.867 289.529 1.00 60.79 ATOM 1103 CB ASN G 339 89.634 149.540 290.787 1.00 63.48 ATOM 1104 CG ASN G 339 88.141 149.642 290.562 1.00 72.33 ATOM 1105 OD1 ASN G 339 87.600 149.024 289.644 1.00 75.78 ATOM 1106 ND2 ASN G 339 87.464 150.431 291.401 1.00 84.53 ATOM 1107 C ASN G 339 90.374 151.367 289.231 1.00 60.15 ATOM 1108 O ASN G 339 89.708 151.781 288.285 1.00 59.35 ATOM 1109 N ASN G 340 91.059 152.174 290.043 1.00 60.28 ATOM 1110 CA ASN G 340 91.105 153.626 289.833 1.00 58.67 ATOM 1111 CB ASN G 340 91.831 154.326 290.985 1.00 60.10 ATOM 1112 CG ASN G 340 90.958 154.500 292.207 1.00 60.66 ATOM 1113 OD1 ASN G 340 91.411 154.997 293.238 1.00 74.46 ATOM 1114 ND2 ASN G 340 89.697 154.095 292.100 1.00 62.54 ATOM 1115 C ASN G 340 91.770 153.993 288.513 1.00 57.75 ATOM 1116 O ASN G 340 91.356 154.933 287.835 1.00 53.34 ATOM 1117 N THR G 341 92.810 153.245 288.160 1.00 59.08 ATOM 1118 CA THR G 341 93.490 153.423 286.886 1.00 60.31 ATOM 1119 CB THR G 341 94.634 152.404 286.717 1.00 62.02 ATOM 1120 OG1 THR G 341 95.623 152.632 287.729 1.00 67.40 ATOM 1121 CG2 THR G 341 95.282 152.530 285.353 1.00 64.37 ATOM 1122 C THR G 341 92.493 153.305 285.737 1.00 57.42 ATOM 1123 O THR G 341 92.365 154.221 284.931 1.00 57.66 ATOM 1124 N LEU G 342 91.775 152.188 285.678 1.00 57.86 ATOM 1125 CA LEU G 342 90.764 151.980 284.640 1.00 57.05 ATOM 1126 CB LEU G 342 90.066 150.630 284.823 1.00 55.57 ATOM 1127 CG LEU G 342 90.916 149.368 284.689 1.00 58.40 ATOM 1128 CD1 LEU G 342 90.086 148.122 284.978 1.00 58.24 ATOM 1129 CD2 LEU G 342 91.540 149.291 283.307 1.00 51.49 ATOM 1130 C LEU G 342 89.725 153.104 284.618 1.00 55.80 ATOM 1131 O LEU G 342 89.342 153.580 283.553 1.00 57.64 ATOM 1132 N LYS G 343 89.272 153.516 285.797 1.00 55.09 ATOM 1133 CA LYS G 343 88.298 154.598 285.915 1.00 57.53 ATOM 1134 CB LYS G 343 87.904 154.808 287.386 1.00 56.79 ATOM 1135 CG LYS G 343 87.118 156.085 287.688 1.00 54.53 ATOM 1136 CD LYS G 343 88.030 157.158 288.282 1.00 73.25 ATOM 1137 CE LYS G 343 87.245 158.339 288.848 1.00 76.21 ATOM 1138 NZ LYS G 343 86.764 159.268 287.788 1.00 76.58 ATOM 1139 C LYS G 343 88.815 155.893 285.286 1.00 58.84 ATOM 1140 O LYS G 343 88.059 156.615 284.636 1.00 61.58 ATOM 1141 N GLN G 344 90.103 156.175 285.474 1.00 58.11 ATOM 1142 CA GLN G 344 90.720 157.371 284.904 1.00 59.44 ATOM 1143 CB GLN G 344 92.048 157.687 285.605 1.00 58.54 ATOM 1144 CG GLN G 344 91.898 158.152 287.054 1.00 56.16 ATOM 1145 CD GLN G 344 93.236 158.384 287.743 1.00 60.72 ATOM 1146 OE1 GLN G 344 94.274 157.896 287.295 1.00 65.78 ATOM 1147 NE2 GLN G 344 93.214 159.134 288.842 1.00 69.49 ATOM 1148 C GLN G 344 90.931 157.235 283.396 1.00 58.98 ATOM 1149 O GLN G 344 90.793 158.203 282.653 1.00 64.06 ATOM 1150 N ILE G 345 91.263 156.030 282.951 1.00 59.20 ATOM 1151 CA ILE G 345 91.463 155.762 281.525 1.00 58.60 ATOM 1152 CB ILE G 345 92.142 154.403 281.303 1.00 58.65 ATOM 1153 CG1 ILE G 345 93.516 154.391 281.970 1.00 54.49 ATOM 1154 CD1 ILE G 345 94.130 153.028 282.051 1.00 50.19 ATOM 1155 CG2 ILE G 345 92.269 154.101 279.814 1.00 62.09 ATOM 1156 C ILE G 345 90.147 155.816 280.750 1.00 55.16 ATOM 1157 O ILE G 345 90.052 156.477 279.716 1.00 56.25 ATOM 1158 N ALA G 346 89.135 155.121 281.262 1.00 54.27 ATOM 1159 CA ALA G 346 87.800 155.149 280.674 1.00 52.73 ATOM 1160 CB ALA G 346 86.862 154.260 281.468 1.00 52.30 ATOM 1161 C ALA G 346 87.255 156.576 280.614 1.00 54.51 ATOM 1162 O ALA G 346 86.504 156.932 279.703 1.00 56.37 ATOM 1163 N SER G 347 87.643 157.389 281.590 1.00 52.32 ATOM 1164 CA SER G 347 87.198 158.769 281.661 1.00 53.87 ATOM 1165 CB SER G 347 87.573 159.372 283.015 1.00 52.42 ATOM 1166 OG SER G 347 86.707 160.438 283.345 1.00 54.90 ATOM 1167 C SER G 347 87.793 159.599 280.521 1.00 54.61 ATOM 1168 O SER G 347 87.105 160.425 279.920 1.00 54.01 ATOM 1169 N LYS G 348 89.072 159.371 280.232 1.00 54.81 ATOM 1170 CA LYS G 348 89.739 160.025 279.109 1.00 55.30 ATOM 1171 CB LYS G 348 91.255 159.823 279.187 1.00 53.00 ATOM 1172 CG LYS G 348 91.948 160.704 280.206 1.00 54.40 ATOM 1173 CD LYS G 348 91.774 162.176 279.862 1.00 49.48 ATOM 1174 CE LYS G 348 92.073 163.060 281.053 1.00 35.62 ATOM 1175 NZ LYS G 348 91.811 164.481 280.740 1.00 52.25 ATOM 1176 C LYS G 348 89.212 159.514 277.765 1.00 57.17 ATOM 1177 O LYS G 348 88.997 160.292 276.837 1.00 61.08 ATOM 1178 N LEU G 349 89.006 158.205 277.663 1.00 56.49 ATOM 1179 CA LEU G 349 88.499 157.613 276.431 1.00 57.83 ATOM 1180 CB LEU G 349 88.457 156.087 276.543 1.00 52.08 ATOM 1181 CG LEU G 349 89.833 155.417 276.603 1.00 54.70 ATOM 1182 CD1 LEU G 349 89.729 153.934 276.941 1.00 57.44 ATOM 1183 CD2 LEU G 349 90.593 155.604 275.296 1.00 53.07 ATOM 1184 C LEU G 349 87.128 158.193 276.075 1.00 59.23 ATOM 1185 O LEU G 349 86.883 158.561 274.924 1.00 60.57 ATOM 1186 N ARG G 350 86.247 158.290 277.069 1.00 62.01 ATOM 1187 CA ARG G 350 84.959 158.965 276.899 1.00 63.31 ATOM 1188 CB ARG G 350 84.223 159.065 278.232 1.00 62.29 ATOM 1189 CG ARG G 350 83.166 158.014 278.479 1.00 67.55 ATOM 1190 CD ARG G 350 82.179 158.538 279.506 1.00 76.43 ATOM 1191 NE ARG G 350 82.868 159.308 280.540 1.00 89.96 ATOM 1192 CZ ARG G 350 82.353 160.363 281.166 1.00 94.10 ATOM 1193 NH1 ARG G 350 81.133 160.790 280.867 1.00 96.94 ATOM 1194 NH2 ARG G 350 83.064 160.997 282.090 1.00 89.30 ATOM 1195 C ARG G 350 85.158 160.374 276.362 1.00 64.04 ATOM 1196 O ARG G 350 84.554 160.767 275.366 1.00 66.33 ATOM 1197 N GLU G 351 86.003 161.133 277.051 1.00 65.15 ATOM 1198 CA GLU G 351 86.326 162.499 276.663 1.00 64.28 ATOM 1199 CB GLU G 351 87.480 163.011 277.530 1.00 66.16 ATOM 1200 CG GLU G 351 88.107 164.313 277.071 1.00 75.54 ATOM 1201 CD GLU G 351 89.589 164.380 277.397 1.00 85.09 ATOM 1202 OE1 GLU G 351 90.325 163.437 277.025 1.00 87.57 ATOM 1203 OE2 GLU G 351 90.018 165.375 278.019 1.00 83.24 ATOM 1204 C GLU G 351 86.695 162.568 275.183 1.00 60.64 ATOM 1205 O GLU G 351 86.455 163.571 274.515 1.00 56.91 ATOM 1206 N GLN G 352 87.269 161.484 274.675 1.00 61.32 ATOM 1207 CA GLN G 352 87.711 161.424 273.288 1.00 62.93 ATOM 1208 CB GLN G 352 88.961 160.547 273.175 1.00 61.07 ATOM 1209 CG GLN G 352 89.504 160.409 271.767 1.00 62.34 ATOM 1210 CD GLN G 352 89.922 161.734 271.169 1.00 70.35 ATOM 1211 OE1 GLN G 352 89.513 162.081 270.060 1.00 70.22 ATOM 1212 NE2 GLN G 352 90.738 162.489 271.905 1.00 65.60 ATOM 1213 C GLN G 352 86.619 160.925 272.334 1.00 63.59 ATOM 1214 O GLN G 352 86.521 161.388 271.199 1.00 65.76 ATOM 1215 N PHE G 353 85.798 159.987 272.796 1.00 62.52 ATOM 1216 CA PHE G 353 84.809 159.349 271.926 1.00 61.51 ATOM 1217 CB PHE G 353 84.959 157.825 271.990 1.00 59.88 ATOM 1218 CG PHE G 353 86.235 157.323 271.382 1.00 54.07 ATOM 1219 CD1 PHE G 353 87.354 157.108 272.164 1.00 56.57 ATOM 1220 CE1 PHE G 353 88.534 156.657 271.602 1.00 53.98 ATOM 1221 CZ PHE G 353 88.600 156.420 270.244 1.00 55.90 ATOM 1222 CE2 PHE G 353 87.489 156.631 269.455 1.00 44.88 ATOM 1223 CD2 PHE G 353 86.319 157.084 270.020 1.00 54.18 ATOM 1224 C PHE G 353 83.358 159.759 272.198 1.00 63.71 ATOM 1225 O PHE G 353 82.438 159.263 271.550 1.00 59.61 ATOM 1226 N GLY G 354 83.157 160.668 273.148 1.00 69.88 ATOM 1227 CA GLY G 354 81.811 161.121 273.505 1.00 76.02 ATOM 1228 C GLY G 354 81.481 160.818 274.955 1.00 78.04 ATOM 1229 O GLY G 354 81.728 159.712 275.438 1.00 80.33 ATOM 1230 N ASN G 355 80.915 161.800 275.649 1.00 79.00 ATOM 1231 CA ASN G 355 80.677 161.694 277.089 1.00 81.17 ATOM 1232 CB ASN G 355 80.349 163.069 277.681 1.00 81.75 ATOM 1233 CG ASN G 355 81.523 164.032 277.612 1.00 83.47 ATOM 1234 OD1 ASN G 355 82.671 163.625 277.422 1.00 77.60 ATOM 1235 ND2 ASN G 355 81.237 165.321 277.770 1.00 88.22 ATOM 1236 C ASN G 355 79.607 160.680 277.502 1.00 82.14 ATOM 1237 O ASN G 355 79.552 160.273 278.664 1.00 82.10 ATOM 1238 N ASN G 356 78.761 160.273 276.561 1.00 81.97 ATOM 1239 CA ASN G 356 77.721 159.292 276.865 1.00 82.64 ATOM 1240 CB ASN G 356 76.378 159.699 276.251 1.00 85.05 ATOM 1241 CG ASN G 356 75.480 160.421 277.240 1.00 93.29 ATOM 1242 OD1 ASN G 356 74.377 159.961 277.539 1.00 100.46 ATOM 1243 ND2 ASN G 356 75.953 161.552 277.761 1.00 107.24 ATOM 1244 C ASN G 356 78.084 157.866 276.462 1.00 78.84 ATOM 1245 O ASN G 356 77.254 156.960 276.543 1.00 78.14 ATOM 1246 N LYS G 357 79.329 157.672 276.042 1.00 74.83 ATOM 1247 CA LYS G 357 79.804 156.351 275.650 1.00 69.22 ATOM 1248 CB LYS G 357 81.036 156.467 274.747 1.00 70.31 ATOM 1249 CG LYS G 357 80.749 157.004 273.352 1.00 71.45 ATOM 1250 CD LYS G 357 79.909 156.028 272.541 1.00 67.89 ATOM 1251 CE LYS G 357 79.729 156.502 271.105 1.00 67.07 ATOM 1252 NZ LYS G 357 81.018 156.517 270.363 1.00 64.51 ATOM 1253 C LYS G 357 80.132 155.484 276.861 1.00 64.68 ATOM 1254 O LYS G 357 80.848 155.910 277.767 1.00 65.28 ATOM 1255 N THR G 358 79.591 154.271 276.873 1.00 57.32 ATOM 1256 CA THR G 358 79.985 153.261 277.842 1.00 52.81 ATOM 1257 CB THR G 358 78.954 152.122 277.904 1.00 52.09 ATOM 1258 OG1 THR G 358 77.714 152.634 278.402 1.00 44.17 ATOM 1259 CG2 THR G 358 79.430 150.993 278.807 1.00 47.62 ATOM 1260 C THR G 358 81.330 152.707 277.402 1.00 54.23 ATOM 1261 O THR G 358 81.518 152.382 276.232 1.00 56.26 ATOM 1262 N ILE G 359 82.275 152.627 278.329 1.00 56.52 ATOM 1263 CA ILE G 359 83.616 152.170 278.000 1.00 53.22 ATOM 1264 CB ILE G 359 84.693 153.087 278.613 1.00 56.22 ATOM 1265 CG1 ILE G 359 84.555 154.523 278.081 1.00 52.74 ATOM 1266 CD1 ILE G 359 84.680 154.657 276.552 1.00 42.86 ATOM 1267 CG2 ILE G 359 86.088 152.519 278.359 1.00 49.87 ATOM 1268 C ILE G 359 83.804 150.758 278.518 1.00 56.11 ATOM 1269 O ILE G 359 83.741 150.527 279.727 1.00 54.85 ATOM 1270 N ILE G 360 84.028 149.820 277.600 1.00 54.33 ATOM 1271 CA ILE G 360 84.160 148.407 277.939 1.00 53.18 ATOM 1272 CB ILE G 360 83.220 147.536 277.091 1.00 51.88 ATOM 1273 CG1 ILE G 360 81.771 148.012 277.212 1.00 54.49 ATOM 1274 CD1 ILE G 360 80.823 147.306 276.259 1.00 46.69 ATOM 1275 CG2 ILE G 360 83.348 146.077 277.498 1.00 48.25 ATOM 1276 C ILE G 360 85.570 147.892 277.688 1.00 55.79 ATOM 1277 O ILE G 360 86.115 148.061 276.598 1.00 58.55 ATOM 1278 N PHE G 361 86.150 147.245 278.691 1.00 57.18 ATOM 1279 CA PHE G 361 87.439 146.595 278.528 1.00 55.50 ATOM 1280 CB PHE G 361 88.357 146.911 279.710 1.00 57.64 ATOM 1281 CG PHE G 361 88.718 148.368 279.829 1.00 59.77 ATOM 1282 CD1 PHE G 361 88.165 149.154 280.825 1.00 61.48 ATOM 1283 CE1 PHE G 361 88.496 150.495 280.940 1.00 52.45 ATOM 1284 CZ PHE G 361 89.388 151.062 280.055 1.00 55.91 ATOM 1285 CE2 PHE G 361 89.950 150.290 279.053 1.00 53.64 ATOM 1286 CD2 PHE G 361 89.614 148.950 278.944 1.00 67.14 ATOM 1287 C PHE G 361 87.253 145.088 278.381 1.00 57.68 ATOM 1288 O PHE G 361 86.646 144.439 279.238 1.00 59.68 ATOM 1289 N LYS G 362 87.765 144.541 277.280 1.00 58.22 ATOM 1290 CA LYS G 362 87.717 143.103 277.025 1.00 55.95 ATOM 1291 CB LYS G 362 86.827 142.793 275.827 1.00 56.69 ATOM 1292 CG LYS G 362 85.358 143.044 276.065 1.00 60.06 ATOM 1293 CD LYS G 362 84.532 142.606 274.871 1.00 64.37 ATOM 1294 CE LYS G 362 83.055 142.892 275.090 1.00 75.02 ATOM 1295 NZ LYS G 362 82.592 142.440 276.434 1.00 81.57 ATOM 1296 C LYS G 362 89.116 142.546 276.777 1.00 61.09 ATOM 1297 O LYS G 362 90.056 143.294 276.494 1.00 60.22 ATOM 1298 N GLN G 363 89.245 141.227 276.882 1.00 61.38 ATOM 1299 CA GLN G 363 90.532 140.569 276.736 1.00 64.08 ATOM 1300 CB GLN G 363 90.433 139.102 277.168 1.00 56.34 ATOM 1301 CG GLN G 363 89.735 132.221 276.153 1.00 71.68 ATOM 1302 CD GLN G 363 89.178 136.955 276.757 1.00 70.70 ATOM 1303 OE1 GLN G 363 88.247 136.996 277.559 1.00 76.44 ATOM 1304 NE2 GLN G 363 89.734 135.817 276.362 1.00 74.08 ATOM 1305 C GLN G 363 91.019 140.653 275.289 1.00 67.53 ATOM 1306 O GLN G 363 90.224 140.809 274.358 1.00 65.51 ATOM 1307 N SER G 364 92.331 140.544 275.118 1.00 69.60 ATOM 1308 CA SER G 364 92.956 140.539 273.801 1.00 71.67 ATOM 1309 CB SER G 364 94.471 140.396 273.953 1.00 73.79 ATOM 1310 OG SER G 364 95.104 140.273 272.693 1.00 80.62 ATOM 1311 C SER G 364 92.420 139.411 272.925 1.00 67.46 ATOM 1312 O SER G 364 91.960 138.391 273.424 1.00 68.43 ATOM 1313 N SER G 365 92.465 139.612 271.613 1.00 68.39 ATOM 1314 CA SER G 365 92.141 138.554 270.669 1.00 66.75 ATOM 1315 CB SER G 365 90.791 138.815 270.003 1.00 65.72 ATOM 1316 OG SER G 365 90.373 137.672 269.280 1.00 66.11 ATOM 1317 C SER G 365 93.254 138.475 269.630 1.00 63.91 ATOM 1318 O SER G 365 93.648 139.495 269.061 1.00 65.87 ATOM 1319 N GLY G 366 93.767 137.270 269.391 1.00 60.71 ATOM 1320 CA GLY G 366 94.945 137.102 268.540 1.00 55.00 ATOM 1321 C GLY G 366 95.387 135.661 268.376 1.00 57.44 ATOM 1322 O GLY G 366 94.831 134.757 269.003 1.00 58.30 ATOM 1323 N GLY G 367 96.396 135.445 267.533 1.00 53.41 ATOM 1324 CA GLY G 367 96.836 134.095 267.203 1.00 55.31 ATOM 1325 C GLY G 367 98.188 133.690 267.778 1.00 53.90 ATOM 1326 O GLY G 367 98.732 132.653 267.410 1.00 54.48 ATOM 1327 N ASP G 368 98.730 134.502 268.679 1.00 56.07 ATOM 1328 CA ASP G 368 99.986 134.169 269.356 1.00 57.85 ATOM 1329 CB ASP G 368 101.192 134.683 268.560 1.00 52.96 ATOM 1330 CG ASP G 368 101.589 133.741 267.438 1.00 60.29 ATOM 1331 OD1 ASP G 368 101.598 134.185 266.275 1.00 66.18 ATOM 1332 OD2 ASP G 368 101.874 132.549 267.714 1.00 53.79 ATOM 1333 C ASP G 368 100.026 134.688 270.790 1.00 55.75 ATOM 1334 O ASP G 368 99.413 135.705 271.098 1.00 52.88 ATOM 1335 N PRO G 369 100.740 133.973 271.679 1.00 57.98 ATOM 1336 CA PRO G 369 100.864 134.402 273.075 1.00 55.42 ATOM 1337 CB PRO G 369 101.718 133.297 273.719 1.00 57.65 ATOM 1338 CG PRO G 369 102.372 132.581 272.580 1.00 59.67 ATOM 1339 CD PRO G 369 101.439 132.701 271.418 1.00 54.08 ATOM 1340 C PRO G 369 101.541 135.761 273.226 1.00 58.71 ATOM 1341 O PRO G 369 101.264 136.478 274.187 1.00 58.67 ATOM 1342 N GLU G 370 102.411 136.118 272.283 1.00 59.11 ATOM 1343 CA GLU G 370 103.110 137.402 272.333 1.00 61.36 ATOM 1344 CB GLU G 370 104.161 137.486 271.224 1.00 60.44 ATOM 1345 CG GLU G 370 105.428 136.695 271.496 1.00 61.27 ATOM 1346 CD GLU G 370 105.238 135.201 271.342 1.00 62.65 ATOM 1347 OE1 GLU G 370 106.096 134.442 271.831 1.00 68.96 ATOM 1348 OE2 GLU G 370 104.234 134.782 270.732 1.00 63.39 ATOM 1349 C GLU G 370 102.133 138.565 272.201 1.00 65.29 ATOM 1350 O GLU G 370 102.436 139.694 272.583 1.00 65.80 ATOM 1351 N ILE G 371 100.961 138.275 271.646 1.00 65.77 ATOM 1352 CA ILE G 371 99.925 139.278 271.434 1.00 66.11 ATOM 1353 CB ILE G 371 99.221 139.057 270.073 1.00 65.75 ATOM 1354 CG1 ILE G 371 100.214 139.225 268.921 1.00 69.39 ATOM 1355 CD1 ILE G 371 99.758 138.596 267.614 1.00 70.25 ATOM 1356 CG2 ILE G 371 98.063 140.015 269.908 1.00 66.85 ATOM 1357 C ILE G 371 98.880 139.195 272.538 1.00 65.01 ATOM 1358 O ILE G 371 98.518 140.204 273.148 1.00 63.43 ATOM 1359 N VAL G 372 98.420 137.971 272.787 1.00 62.74 ATOM 1360 CA VAL G 372 97.305 137.684 273.684 1.00 63.16 ATOM 1361 CB VAL G 372 96.833 136.214 273.500 1.00 61.48 ATOM 1362 CG1 VAL G 372 95.823 135.824 274.562 1.00 66.88 ATOM 1363 CG2 VAL G 372 96.250 136.020 272.108 1.00 67.94 ATOM 1364 C VAL G 372 97.617 137.940 275.159 1.00 61.60 ATOM 1365 O VAL G 372 96.768 138.432 275.903 1.00 66.24 ATOM 1366 N THR G 373 98.829 137.591 275.580 1.00 63.42 ATOM 1367 CA THR G 373 99.244 137.781 276.965 1.00 63.80 ATOM 1368 CB THR G 373 100.202 136.666 277.436 1.00 60.84 ATOM 1369 OG1 THR G 373 101.517 136.910 276.919 1.00 56.82 ATOM 1370 CG2 THR G 373 99.726 135.301 276.978 1.00 52.18 ATOM 1371 C THR G 373 99.990 139.109 277.068 1.00 67.16 ATOM 1372 O THR G 373 100.477 139.633 276.059 1.00 66.29 ATOM 1373 N HIS G 374 100.080 139.659 278.273 1.00 65.45 ATOM 1374 CA HIS G 374 101.014 140.751 278.473 1.00 64.51 ATOM 1375 CB HIS G 374 100.770 141.524 279.760 1.00 61.47 ATOM 1376 CG HIS G 374 101.890 142.458 280.097 1.00 58.83 ATOM 1377 ND1 HIS G 374 102.246 143.511 279.281 1.00 63.65 ATOM 1378 CE1 HIS G 374 103.272 144.151 279.815 1.00 63.96 ATOM 1379 NE2 HIS G 374 103.599 143.545 280.942 1.00 67.00 ATOM 1380 CD2 HIS G 374 102.754 142.480 281.139 1.00 59.28 ATOM 1381 C HIS G 374 102.401 140.139 278.501 1.00 64.00 ATOM 1382 O HIS G 374 102.760 139.428 279.440 1.00 58.86 ATOM 1383 N TRP G 375 103.165 140.414 277.452 1.00 60.54 ATOM 1384 CA TRP G 375 104.453 139.788 277.248 1.00 59.59 ATOM 1385 CB TRP G 375 104.473 139.143 275.867 1.00 59.28 ATOM 1386 CG TRP G 375 105.779 138.574 275.445 1.00 58.70 ATOM 1387 CD1 TRP G 375 106.520 137.637 276.102 1.00 63.55 ATOM 1388 NE1 TRP G 375 107.655 137.346 275.386 1.00 66.26 ATOM 1389 CE2 TRP G 375 107.659 138.090 274.235 1.00 63.35 ATOM 1390 CD2 TRP G 375 106.487 138.871 274.234 1.00 65.10 ATOM 1391 CE3 TRP G 375 106.247 139.734 273.155 1.00 65.33 ATOM 1392 CZ3 TRP G 375 107.177 139.785 272.125 1.00 64.20 ATOM 1393 CH2 TRP G 375 108.337 138.994 272.155 1.00 59.32 ATOM 1394 CZ2 TRP G 375 108.596 138.144 273.198 1.00 60.91 ATOM 1395 C TRP G 375 105.546 140.832 277.376 1.00 59.31 ATOM 1396 O TRP G 375 105.587 141.796 276.609 1.00 60.83 ATOM 1397 N PHE G 376 106.421 140.651 278.359 1.00 57.96 ATOM 1398 CA PHE G 376 107.494 141.613 278.597 1.00 55.65 ATOM 1399 CB PHE G 376 107.044 142.692 279.582 1.00 53.59 ATOM 1400 CG PHE G 376 106.986 142.230 281.014 1.00 53.18 ATOM 1401 CD1 PHE G 376 105.917 141.482 281.476 1.00 54.44 ATOM 1402 CE1 PHE G 376 105.861 141.063 282.799 1.00 56.57 ATOM 1403 CZ PHE G 376 106.874 141.398 283.673 1.00 55.67 ATOM 1404 CE2 PHE G 376 107.942 142.151 283.227 1.00 49.92 ATOM 1405 CD2 PHE G 376 107.994 142.566 281.907 1.00 52.19 ATOM 1406 C PHE G 376 108.744 140.930 279.112 1.00 55.62 ATOM 1407 O PHE G 376 108.684 139.800 279.597 1.00 58.91 ATOM 1408 N ASN G 377 109.878 141.616 279.006 1.00 55.47 ATOM 1409 CA ASN G 377 111.125 141.078 279.529 1.00 56.89 ATOM 1410 CB ASN G 377 112.180 140.942 278.431 1.00 55.37 ATOM 1411 CG ASN G 377 112.719 142.278 277.978 1.00 55.83 ATOM 1412 OD1 ASN G 377 111.989 143.098 277.425 1.00 52.08 ATOM 1413 ND2 ASN G 377 114.001 142.506 278.212 1.00 51.40 ATOM 1414 C ASN G 377 111.682 141.901 280.684 1.00 60.96 ATOM 1415 O ASN G 377 111.721 143.133 280.635 1.00 58.30 ATOM 1416 N CYS G 378 112.095 141.199 281.730 1.00 62.89 ATOM 1417 CA CYS G 378 112.782 141.799 282.848 1.00 64.11 ATOM 1418 CB CYS G 378 112.104 141.386 284.149 1.00 65.63 ATOM 1419 SG CYS G 378 112.407 142.477 285.555 1.00 72.07 ATOM 1420 C CYS G 378 114.183 141.226 282.778 1.00 63.03 ATOM 1421 O CYS G 378 114.443 140.150 283.310 1.00 63.31 ATOM 1422 N GLY G 379 115.075 141.931 282.089 1.00 62.27 ATOM 1423 CA GLY G 379 116.392 141.385 281.767 1.00 61.32 ATOM 1424 C GLY G 379 116.290 140.352 280.658 1.00 60.16 ATOM 1425 O GLY G 379 115.724 140.618 279.597 1.00 61.95 ATOM 1426 N GLY G 380 116.828 139.164 280.907 1.00 61.37 ATOM 1427 CA GLY G 380 116.793 138.078 279.931 1.00 61.12 ATOM 1428 C GLY G 380 115.665 137.097 280.185 1.00 61.70 ATOM 1429 O GLY G 380 115.535 136.093 279.485 1.00 61.10 ATOM 1430 N GLU G 381 114.849 137.387 281.194 1.00 61.89 ATOM 1431 CA GLU G 381 113.699 136.554 281.512 1.00 60.86 ATOM 1432 CB GLU G 381 113.545 136.393 283.028 1.00 62.71 ATOM 1433 CG GLU G 381 114.857 136.248 283.790 1.00 64.60 ATOM 1434 CD GLU G 381 115.558 134.927 283.531 1.00 75.27 ATOM 1435 OE1 GLU G 381 114.877 133.953 283.147 1.00 79.63 ATOM 1436 OE2 GLU G 381 116.792 134.862 283.721 1.00 73.77 ATOM 1437 C GLU G 381 112.445 137.191 280.931 1.00 62.52 ATOM 1438 O GLU G 381 112.171 138.369 281.181 1.00 62.19 ATOM 1439 N PHE G 382 111.692 136.415 280.152 1.00 57.30 ATOM 1440 CA PHE G 382 110.470 136.905 279.525 1.00 57.74 ATOM 1441 CB PHE G 382 110.413 136.502 278.050 1.00 52.94 ATOM 1442 CG PHE G 382 111.330 137.296 277.169 1.00 56.57 ATOM 1443 CD1 PHE G 382 110.820 138.220 276.273 1.00 54.34 ATOM 1444 CE1 PHE G 382 111.662 138.956 275.458 1.00 56.65 ATOM 1445 CZ PHE G 382 113.033 138.775 275.538 1.00 53.70 ATOM 1446 CE2 PHE G 382 113.556 137.860 276.431 1.00 55.38 ATOM 1447 CD2 PHE G 382 112.707 137.126 277.241 1.00 57.78 ATOM 1448 C PHE G 382 109.246 136.371 280.246 1.00 61.27 ATOM 1449 O PHE G 382 109.129 135.166 280.481 1.00 65.55 ATOM 1450 N PHE G 383 108.334 137.272 280.594 1.00 59.89 ATOM 1451 CA PHE G 383 107.110 136.887 281.279 1.00 60.27 ATOM 1452 CB PHE G 383 106.825 137.834 282.451 1.00 56.55 ATOM 1453 CG PHE G 383 107.848 137.777 283.558 1.00 60.63 ATOM 1454 CD1 PHE G 383 109.084 138.396 283.422 1.00 44.66 ATOM 1455 CE1 PHE G 383 110.014 138.350 284.439 1.00 51.79 ATOM 1456 CZ PHE G 383 109.716 137.696 285.615 1.00 57.34 ATOM 1457 CE2 PHE G 383 108.486 137.085 285.770 1.00 55.22 ATOM 1458 CD2 PHE G 383 107.559 137.132 284.751 1.00 52.17 ATOM 1459 C PHE G 383 105.937 136.919 280.308 1.00 59.90 ATOM 1460 O PHE G 383 105.699 137.933 279.651 1.00 63.76 ATOM 1461 N TYR G 384 105.211 135.810 280.213 1.00 60.02 ATOM 1462 CA TYR G 384 103.945 135.780 279.479 1.00 58.10 ATOM 1463 CB TYR G 384 103.847 134.541 278.590 1.00 58.50 ATOM 1464 CG TYR G 384 104.755 134.521 277.381 1.00 59.44 ATOM 1465 CD1 TYR G 384 106.074 134.084 277.479 1.00 64.21 ATOM 1466 CE1 TYR G 384 106.902 134.049 276.367 1.00 60.68 ATOM 1467 CZ TYR G 384 106.406 134.441 275.137 1.00 61.54 ATOM 1468 OH TYR G 384 107.213 134.413 274.024 1.00 58.77 ATOM 1469 CE2 TYR G 384 105.103 134.869 275.016 1.00 61.92 ATOM 1470 CD2 TYR G 384 104.284 134.902 276.133 1.00 64.55 ATOM 1471 C TYR G 384 102.816 135.743 280.500 1.00 59.00 ATOM 1472 O TYR G 384 102.528 134.690 281.076 1.00 57.42 ATOM 1473 N CYS G 385 102.180 136.890 280.728 1.00 56.92 ATOM 1474 CA CYS G 385 101.178 137.000 281.786 1.00 58.48 ATOM 1475 CB CYS G 385 101.465 138.212 282.675 1.00 55.77 ATOM 1476 SG CYS G 385 102.983 138.054 283.617 1.00 66.41 ATOM 1477 C CYS G 385 99.749 137.056 281.265 1.00 57.22 ATOM 1478 O CYS G 385 99.405 137.915 280.458 1.00 57.84 ATOM 1479 N ASN G 386 98.924 136.128 281.740 1.00 58.12 ATOM 1480 CA ASN G 386 97.505 136.101 281.400 1.00 60.64 ATOM 1481 CB ASN G 386 96.885 134.812 281.938 1.00 56.39 ATOM 1482 CG ASN G 386 95.432 134.650 281.554 1.00 58.49 ATOM 1483 OD1 ASN G 386 94.698 135.632 281.414 1.00 57.72 ATOM 1484 ND2 ASN G 386 95.003 133.390 281.387 1.00 60.20 ATOM 1485 C ASN G 386 96.810 137.334 281.982 1.00 61.93 ATOM 1486 O ASN G 386 96.646 137.454 283.201 1.00 62.66 ATOM 1487 N SER G 387 96.412 138.253 281.109 1.00 60.80 ATOM 1488 CA SER G 387 95.931 139.564 281.545 1.00 62.64 ATOM 1489 CB SER G 387 96.575 140.675 280.708 1.00 62.04 ATOM 1490 OG SER G 387 96.108 140.640 279.367 1.00 64.55 ATOM 1491 C SER G 387 94.412 139.702 281.510 1.00 62.08 ATOM 1492 O SER G 387 93.885 140.804 281.624 1.00 64.62 ATOM 1493 N THR G 388 93.709 138.585 281.365 1.00 59.98 ATOM 1494 CA THR G 388 92.252 138.614 281.325 1.00 60.62 ATOM 1495 CB THR G 388 91.668 137.199 281.280 1.00 58.22 ATOM 1496 OG1 THR G 388 92.164 136.521 280.120 1.00 64.59 ATOM 1497 CG2 THR G 388 90.150 137.249 281.231 1.00 55.50 ATOM 1498 C THR G 388 91.637 139.378 282.504 1.00 63.43 ATOM 1499 O THR G 388 90.665 140.117 282.325 1.00 64.09 ATOM 1500 N GLN G 389 92.207 139.202 283.697 1.00 61.27 ATOM 1501 CA GLN G 389 91.676 139.818 284.915 1.00 60.13 ATOM 1502 CB GLN G 389 92.364 139.253 286.157 1.00 59.62 ATOM 1503 CG GLN G 389 92.218 137.761 286.347 1.00 49.46 ATOM 1504 CD GLN G 389 92.924 137.283 287.598 1.00 57.02 ATOM 1505 OE1 GLN G 389 92.429 137.463 288.710 1.00 53.46 ATOM 1506 NE2 GLN G 389 94.089 136.670 287.424 1.00 59.28 ATOM 1507 C GLN G 389 91.805 141.336 284.932 1.00 60.32 ATOM 1508 O GLN G 389 91.035 142.014 285.607 1.00 64.43 ATOM 1509 N LEU G 390 92.780 141.869 284.202 1.00 61.56 ATOM 1510 CA LEU G 390 92.974 143.316 284.141 1.00 62.02 ATOM 1511 CB LEU G 390 94.417 143.660 283.762 1.00 60.30 ATOM 1512 CG LEU G 390 95.556 143.233 284.691 1.00 62.32 ATOM 1513 CD1 LEU G 390 96.867 143.817 284.191 1.00 65.68 ATOM 1514 CD2 LEU G 390 95.304 143.646 286.133 1.00 60.38 ATOM 1515 C LEU G 390 92.010 143.999 283.166 1.00 62.56 ATOM 1516 O LEU G 390 91.728 145.189 283.295 1.00 62.78 ATOM 1517 N PHE G 391 91.502 143.239 282.201 1.00 63.40 ATOM 1518 CA PHE G 391 90.684 143.802 281.128 1.00 63.96 ATOM 1519 CB PHE G 391 91.481 143.846 279.822 1.00 60.14 ATOM 1520 CG PHE G 391 92.746 144.645 279.928 1.00 64.74 ATOM 1521 CD1 PHE G 391 93.962 144.021 280.158 1.00 63.61 ATOM 1522 CE1 PHE G 391 95.128 144.761 280.268 1.00 66.43 ATOM 1523 CZ PHE G 391 95.087 146.142 280.162 1.00 61.07 ATOM 1524 CE2 PHE G 391 93.880 146.776 279.942 1.00 57.00 ATOM 1525 CD2 PHE G 391 92.716 146.027 279.825 1.00 59.64 ATOM 1526 C PHE G 391 89.378 143.041 280.954 1.00 63.03 ATOM 1527 O PHE G 391 89.195 142.291 279.992 1.00 63.39 ATOM 1528 N ASN G 392 88.469 143.267 281.895 1.00 60.57 ATOM 1529 CA ASN G 392 87.229 142.523 281.987 1.00 64.09 ATOM 1530 CB ASN G 392 87.512 141.169 282.639 1.00 64.87 ATOM 1531 CG ASN G 392 86.265 140.334 282.853 1.00 73.09 ATOM 1532 OD1 ASN G 392 85.271 140.462 282.133 1.00 72.13 ATOM 1533 ND2 ASN G 392 86.326 139.451 283.847 1.00 82.68 ATOM 1534 C ASN G 392 86.203 143.330 282.788 1.00 64.61 ATOM 1535 O ASN G 392 85.646 142.854 283.778 1.00 64.12 ATOM 1536 N SER G 393 85.970 144.566 282.352 1.00 61.98 ATOM 1537 CA SER G 393 85.044 145.463 283.034 1.00 59.50 ATOM 1538 CB SER G 393 85.778 146.236 284.127 1.00 58.20 ATOM 1539 OG SER G 393 86.873 146.947 283.578 1.00 57.44 ATOM 1540 C SER G 393 84.399 146.447 282.064 1.00 58.63 ATOM 1541 O SER G 393 84.947 146.733 280.998 1.00 58.68 ATOM 1542 N THR G 394 83.228 146.958 282.432 1.00 58.32 ATOM 1543 CA THR G 394 82.574 147.999 281.647 1.00 59.37 ATOM 1544 CB THR G 394 81.271 147.505 280.955 1.00 56.41 ATOM 1545 OG1 THR G 394 80.132 147.852 281.743 1.00 58.87 ATOM 1546 CG2 THR G 394 81.298 146.000 280.741 1.00 58.03 ATOM 1547 C THR G 394 82.302 149.207 282.540 1.00 59.53 ATOM 1548 O THR G 394 81.963 149.059 283.715 1.00 60.60 ATOM 1549 N TRP G 395 82.463 150.401 281.981 1.00 60.44 ATOM 1550 CA TRP G 395 82.418 151.626 282.766 1.00 59.19 ATOM 1551 CB TRP G 395 83.803 152.273 282.795 1.00 58.43 ATOM 1552 CG TRP G 395 84.829 151.387 283.423 1.00 59.03 ATOM 1553 CD1 TRP G 395 85.509 150.361 282.824 1.00 58.47 ATOM 1554 NE1 TRP G 395 86.359 149.768 283.728 1.00 57.45 ATOM 1555 CE2 TRP G 395 86.235 150.403 284.937 1.00 54.56 ATOM 1556 CD2 TRP G 395 85.277 151.428 284.782 1.00 53.90 ATOM 1557 CE3 TRP G 395 84.965 152.233 285.883 1.00 51.85 ATOM 1558 CZ3 TRP G 395 85.609 151.994 287.086 1.00 50.72 ATOM 1559 CH2 TRP G 395 86.560 150.970 287.208 1.00 54.20 ATOM 1560 CZ2 TRP G 395 86.886 150.166 286.150 1.00 57.78 ATOM 1561 C TRP G 395 81.382 152.605 282.239 1.00 63.23 ATOM 1562 O TRP G 395 81.223 152.770 281.030 1.00 63.51 ATOM 1563 N PHE G 396 80.679 153.251 283.163 1.00 67.03 ATOM 1564 CA PHE G 396 79.624 154.200 282.823 1.00 72.32 ATOM 1565 CB PHE G 396 80.180 155.356 281.984 1.00 74.87 ATOM 1566 CG PHE G 396 81.474 155.914 282.513 1.00 76.66 ATOM 1567 CD1 PHE G 396 82.616 155.913 281.732 1.00 75.37 ATOM 1568 CE1 PHE G 396 83.809 156.418 282.217 1.00 78.54 ATOM 1569 CZ PHE G 396 83.875 156.922 283.502 1.00 81.42 ATOM 1570 CE2 PHE G 396 82.745 156.923 284.298 1.00 88.77 ATOM 1571 CD2 PHE G 396 81.553 156.418 283.804 1.00 86.48 ATOM 1572 C PHE G 396 78.465 153.493 282.126 1.00 73.89 ATOM 1573 O PHE G 396 77.990 153.926 281.077 1.00 71.90 ATOM 1574 N ASN G 397 78.019 152.401 282.742 1.00 77.35 ATOM 1575 CA ASN G 397 76.928 151.579 282.236 1.00 82.53 ATOM 1576 CB ASN G 397 77.158 150.128 282.669 1.00 82.84 ATOM 1577 CG ASN G 397 76.389 149.125 281.828 1.00 86.53 ATOM 1578 OD1 ASN G 397 76.445 147.922 282.088 1.00 86.38 ATOM 1579 ND2 ASN G 397 75.666 149.609 280.819 1.00 96.54 ATOM 1580 C ASN G 397 75.574 152.077 282.747 1.00 86.00 ATOM 1581 O ASN G 397 75.319 153.282 282.779 1.00 87.18 ATOM 1582 N SER G 398 74.709 151.146 283.140 1.00 89.76 ATOM 1583 CA SER G 398 73.422 151.478 283.744 1.00 91.59 ATOM 1584 CB SER G 398 72.527 150.241 283.793 1.00 91.37 ATOM 1585 OG SER G 398 73.238 149.111 284.271 1.00 89.91 ATOM 1586 C SER G 398 73.646 152.019 285.150 1.00 94.84 ATOM 1587 O SER G 398 73.310 153.166 285.448 1.00 95.54 ATOM 1588 N THR G 399 74.208 151.175 286.011 1.00 98.09 ATOM 1589 CA THR G 399 74.708 151.608 287.310 1.00 101.30 ATOM 1590 CB THR G 399 74.301 150.628 288.441 1.00 101.29 ATOM 1591 OG1 THR G 399 74.813 151.092 289.698 1.00 100.28 ATOM 1592 CG2 THR G 399 74.825 149.224 288.163 1.00 101.24 ATOM 1593 C THR G 399 76.228 151.727 287.200 1.00 102.84 ATOM 1594 O THR G 399 76.962 150.816 287.585 1.00 103.71 ATOM 1595 N TRP G 400 76.686 152.856 286.660 1.00 104.55 ATOM 1596 CA TRP G 400 78.087 153.019 286.250 1.00 105.50 ATOM 1597 CB TRP G 400 78.411 154.490 285.932 1.00 105.27 ATOM 1598 CG TRP G 400 78.820 155.338 287.102 1.00 105.21 ATOM 1599 CD1 TRP G 400 80.094 155.585 287.528 1.00 104.11 ATOM 1600 NE1 TRP G 400 80.075 156.415 288.623 1.00 105.46 ATOM 1601 CE2 TRP G 400 78.774 156.729 288.920 1.00 105.61 ATOM 1602 CD2 TRP G 400 77.955 156.071 287.979 1.00 105.75 ATOM 1603 CE3 TRP G 400 76.567 156.230 288.066 1.00 105.20 ATOM 1604 CZ3 TRP G 400 76.051 157.029 289.073 1.00 103.66 ATOM 1605 CH2 TRP G 400 76.892 157.670 289.992 1.00 103.27 ATOM 1606 CZ2 TRP G 400 78.252 157.533 289.933 1.00 103.23 ATOM 1607 C TRP G 400 79.090 152.406 287.233 1.00 105.88 ATOM 1608 O TRP G 400 79.113 152.749 288.418 1.00 105.91 ATOM 1609 N SER G 401 79.907 151.486 286.725 1.00 104.80 ATOM 1610 CA SER G 401 80.841 150.733 287.556 1.00 104.34 ATOM 1611 CB SER G 401 80.245 149.370 287.921 1.00 104.80 ATOM 1612 OG SER G 401 79.930 148.622 286.757 1.00 105.06 ATOM 1613 C SER G 401 82.186 150.547 286.860 1.00 103.35 ATOM 1614 O SER G 401 82.847 149.520 287.025 1.00 101.17 ATOM 1615 N GLY G 410 85.239 141.398 295.178 1.00 90.85 ATOM 1616 CA GLY G 410 86.640 141.399 294.767 1.00 89.64 ATOM 1617 C GLY G 410 87.579 141.096 295.920 1.00 88.79 ATOM 1618 O GLY G 410 87.220 141.264 297.087 1.00 87.83 ATOM 1619 N SER G 411 88.788 140.647 295.588 1.00 87.09 ATOM 1620 CA SER G 411 89.788 140.304 296.597 1.00 83.89 ATOM 1621 CB SER G 411 90.536 139.027 296.203 1.00 83.56 ATOM 1622 OG SER G 411 91.197 139.188 294.961 1.00 86.92 ATOM 1623 C SER G 411 90.779 141.441 296.830 1.00 80.81 ATOM 1624 O SER G 411 90.602 142.549 296.326 1.00 81.06 ATOM 1625 N ASP G 412 91.825 141.152 297.596 1.00 77.71 ATOM 1626 CA ASP G 412 92.817 142.152 297.970 1.00 73.83 ATOM 1627 CB ASP G 412 93.633 141.647 299.168 1.00 74.00 ATOM 1628 CG ASP G 412 94.351 142.763 299.908 1.00 74.57 ATOM 1629 OD1 ASP G 412 94.463 142.675 301.150 1.00 64.53 ATOM 1630 OD2 ASP G 412 94.804 143.726 299.253 1.00 75.60 ATOM 1631 C ASP G 412 93.742 142.486 296.797 1.00 70.32 ATOM 1632 O ASP G 412 93.860 143.643 296.393 1.00 68.53 ATOM 1633 N THR G 413 94.389 141.461 296.255 1.00 66.21 ATOM 1634 CA THR G 413 95.379 141.646 295.202 1.00 64.15 ATOM 1635 CB THR G 413 96.770 141.171 295.669 1.00 63.17 ATOM 1636 OG1 THR G 413 97.157 141.896 296.843 1.00 65.21 ATOM 1637 CG2 THR G 413 97.811 141.387 294.584 1.00 60.96 ATOM 1638 C THR G 413 94.994 140.878 293.941 1.00 63.69 ATOM 1639 O THR G 413 94.544 139.735 294.012 1.00 65.57 ATOM 1640 N ILE G 414 95.164 141.512 292.787 1.00 60.42 ATOM 1641 CA ILE G 414 94.986 140.820 291.521 1.00 59.40 ATOM 1642 CB ILE G 414 94.740 141.795 290.354 1.00 56.16 ATOM 1643 CG1 ILE G 414 93.521 142.675 290.635 1.00 57.80 ATOM 1644 CD1 ILE G 414 93.262 143.723 289.567 1.00 56.70 ATOM 1645 CG2 ILE G 414 94.530 141.025 289.063 1.00 62.72 ATOM 1646 C ILE G 414 96.234 139.998 291.230 1.00 59.54 ATOM 1647 O ILE G 414 97.338 140.540 291.148 1.00 59.76 ATOM 1648 N THR G 415 96.054 138.688 291.089 1.00 58.56 ATOM 1649 CA THR G 415 97.162 137.788 290.794 1.00 56.05 ATOM 1650 CB THR G 415 97.205 136.600 291.779 1.00 55.94 ATOM 1651 OG1 THR G 415 97.354 137.086 293.121 1.00 55.13 ATOM 1652 CG2 THR G 415 98.364 135.674 291.446 1.00 49.45 ATOM 1653 C THR G 415 97.062 137.260 289.363 1.00 58.72 ATOM 1654 O THR G 415 96.193 136.444 289.052 1.00 57.74 ATOM 1655 N LEU G 416 97.952 137.743 288.499 1.00 57.45 ATOM 1656 CA LEU G 416 98.030 137.285 287.116 1.00 58.73 ATOM 1657 CB LEU G 416 98.606 138.387 286.226 1.00 53.68 ATOM 1658 CG LEU G 416 97.691 139.437 285.599 1.00 59.63 ATOM 1659 CD1 LEU G 416 96.588 139.878 286.537 1.00 63.12 ATOM 1660 CD2 LEU G 416 98.525 140.626 285.145 1.00 61.13 ATOM 1661 C LEU G 416 98.935 136.066 287.028 1.00 59.70 ATOM 1662 O LEU G 416 100.088 136.118 287.462 1.00 59.45 ATOM 1663 N PRO G 417 98.419 134.956 286.476 1.00 60.02 ATOM 1664 CA PRO G 417 99.305 133.822 286.240 1.00 60.59 ATOM 1665 CB PRO G 417 98.346 132.701 285.839 1.00 61.19 ATOM 1666 CG PRO G 417 97.152 133.398 285.289 1.00 60.11 ATOM 1667 CD PRO G 417 97.035 134.686 286.053 1.00 62.11 ATOM 1668 C PRO G 417 100.252 134.171 285.099 1.00 57.80 ATOM 1669 O PRO G 417 99.858 134.860 284.167 1.00 58.28 ATOM 1670 N CYS G 418 101.500 133.731 285.192 1.00 57.76 ATOM 1671 CA CYS G 418 102.504 134.087 284.202 1.00 56.20 ATOM 1672 CB CYS G 418 103.381 135.241 284.704 1.00 59.86 ATOM 1673 SG CYS G 418 102.496 136.760 285.116 1.00 67.50 ATOM 1674 C CYS G 418 103.390 132.902 283.899 1.00 52.98 ATOM 1675 O CYS G 418 103.777 132.162 284.800 1.00 54.20 ATOM 1676 N ARG G 419 103.704 132.719 282.624 1.00 54.60 ATOM 1677 CA ARG G 419 104.712 131.749 282.226 1.00 55.47 ATOM 1678 CB ARG G 419 104.295 130.989 280.963 1.00 55.53 ATOM 1679 CG ARG G 419 103.875 129.551 281.201 1.00 63.36 ATOM 1680 CD ARG G 419 102.366 129.367 281.252 1.00 66.06 ATOM 1681 NE ARG G 419 101.731 129.730 279.991 1.00 66.40 ATOM 1682 CZ ARG G 419 100.593 129.206 279.545 1.00 72.55 ATOM 1683 NH1 ARG G 419 100.092 129.609 278.386 1.00 69.75 ATOM 1684 NH2 ARG G 419 99.962 128.271 280.246 1.00 57.59 ATOM 1685 C ARG G 419 106.009 132.501 281.989 1.00 53.48 ATOM 1686 O ARG G 419 106.006 133.590 281.412 1.00 54.61 ATOM 1687 N ILE G 420 107.113 131.921 282.439 1.00 49.16 ATOM 1688 CA ILE G 420 108.407 132.572 282.349 1.00 51.04 ATOM 1689 CB ILE G 420 108.976 132.836 283.760 1.00 55.10 ATOM 1690 CG1 ILE G 420 107.998 133.710 284.549 1.00 55.66 ATOM 1691 CD1 ILE G 420 108.126 133.584 286.045 1.00 61.90 ATOM 1692 CG2 ILE G 420 110.361 133.488 283.692 1.00 51.74 ATOM 1693 C ILE G 420 109.384 131.756 281.502 1.00 53.57 ATOM 1694 O ILE G 420 109.549 130.549 281.694 1.00 53.75 ATOM 1695 N LYS G 421 110.015 132.427 280.547 1.00 56.09 ATOM 1696 CA LYS G 421 110.994 131.796 279.677 1.00 56.62 ATOM 1697 CB LYS G 421 110.475 131.745 278.236 1.00 55.51 ATOM 1698 CG LYS G 421 109.157 131.005 278.056 1.00 62.78 ATOM 1699 CD LYS G 421 109.323 129.516 278.313 1.00 72.73 ATOM 1700 CE LYS G 421 108.053 128.751 277.971 1.00 74.84 ATOM 1701 NZ LYS G 421 108.258 127.279 278.073 1.00 72.01 ATOM 1702 C LYS G 421 112.287 132.597 279.731 1.00 54.93 ATOM 1703 O LYS G 421 112.263 133.809 279.914 1.00 59.27 ATOM 1704 N GLN G 422 113.413 131.916 279.572 1.00 54.46 ATOM 1705 CA GLN G 422 114.707 132.578 279.547 1.00 54.14 ATOM 1706 CB GLN G 422 115.649 131.945 280.579 1.00 53.41 ATOM 1707 CG GLN G 422 117.059 132.515 280.572 1.00 56.69 ATOM 1708 CD GLN G 422 117.915 131.991 281.710 1.00 59.22 ATOM 1709 OE1 GLN G 422 117.403 131.559 282.745 1.00 68.27 ATOM 1710 NE2 GLN G 422 119.230 132.028 281.523 1.00 69.72 ATOM 1711 C GLN G 422 115.311 132.484 278.150 1.00 53.01 ATOM 1712 O GLN G 422 115.394 131.398 277.575 1.00 54.89 ATOM 1713 N ILE G 423 115.728 133.623 277.604 1.00 52.02 ATOM 1714 CA ILE G 423 116.390 133.647 276.304 1.00 53.46 ATOM 1715 CB ILE G 423 116.528 135.092 275.755 1.00 56.79 ATOM 1716 CG1 ILE G 423 117.013 135.074 274.304 1.00 55.00 ATOM 1717 CD1 ILE G 423 116.617 136.310 273.523 1.00 52.78 ATOM 1718 CG2 ILE G 423 117.446 135.935 276.640 1.00 55.65 ATOM 1719 C ILE G 423 117.754 132.976 276.407 1.00 54.21 ATOM 1720 O ILE G 423 118.511 133.232 277.343 1.00 57.09 ATOM 1721 N ILE G 424 118.056 132.101 275.453 1.00 52.90 ATOM 1722 CA ILE G 424 119.294 131.329 275.492 1.00 52.14 ATOM 1723 CB ILE G 424 119.031 129.871 275.913 1.00 52.68 ATOM 1724 CG1 ILE G 424 118.043 129.208 274.946 1.00 56.61 ATOM 1725 CD1 ILE G 424 117.881 127.721 275.155 1.00 61.44 ATOM 1726 CG2 ILE G 424 118.495 129.819 277.337 1.00 50.86 ATOM 1727 C ILE G 424 120.003 131.343 274.143 1.00 50.39 ATOM 1728 O ILE G 424 121.097 130.806 274.007 1.00 44.56 ATOM 1729 N ASN G 425 119.365 131.961 273.152 1.00 52.00 ATOM 1730 CA ASN G 425 119.928 132.096 271.810 1.00 53.51 ATOM 1731 CB ASN G 425 120.357 130.731 271.264 1.00 51.76 ATOM 1732 CG ASN G 425 121.513 130.830 270.283 1.00 55.64 ATOM 1733 OD1 ASN G 425 121.849 131.914 269.809 1.00 64.02 ATOM 1734 ND2 ASN G 425 122.130 129.694 269.979 1.00 35.96 ATOM 1735 C ASN G 425 118.913 132.755 270.877 1.00 56.36 ATOM 1736 O ASN G 425 117.818 133.121 271.308 1.00 54.79 ATOM 1737 N MET G 426 119.273 132.914 269.606 1.00 58.10 ATOM 1738 CA MET G 426 118.368 133.520 268.629 1.00 59.62 ATOM 1739 CB MET G 426 118.149 135.002 268.952 1.00 58.17 ATOM 1740 CG MET G 426 119.425 135.837 268.922 1.00 61.08 ATOM 1741 SD MET G 426 119.387 137.266 270.025 1.00 64.39 ATOM 1742 CE MET G 426 119.905 136.520 271.570 1.00 69.95 ATOM 1743 C MET G 426 118.880 133.355 267.199 1.00 59.37 ATOM 1744 O MET G 426 120.079 133.192 266.976 1.00 57.12 ATOM 1745 N TRP G 427 117.961 133.386 266.237 1.00 62.65 ATOM 1746 CA TRP G 427 118.319 133.366 264.820 1.00 66.90 ATOM 1747 CB TRP G 427 117.317 132.531 264.019 1.00 68.57 ATOM 1748 CG TRP G 427 117.044 131.166 264.599 1.00 71.04 ATOM 1749 CD1 TRP G 427 116.008 130.815 265.415 1.00 72.97 ATOM 1750 NE1 TRP G 427 116.086 129.481 265.736 1.00 71.53 ATOM 1751 CE2 TRP G 427 117.186 128.940 265.123 1.00 66.40 ATOM 1752 CD2 TRP G 427 117.815 129.972 264.397 1.00 68.44 ATOM 1753 CE3 TRP G 427 118.975 129.675 263.674 1.00 71.34 ATOM 1754 CZ2 TRP G 427 119.463 128.379 263.702 1.00 71.12 ATOM 1755 CH2 TRP G 427 118.814 127.376 264.434 1.00 70.07 ATOM 1756 CZ2 TRP G 427 117.678 127.637 265.150 1.00 70.24 ATOM 1757 C TRP G 427 118.372 134.801 264.287 1.00 68.40 ATOM 1758 O TRP G 427 117.459 135.590 264.531 1.00 70.43 ATOM 1759 N CYS G 428 119.433 135.129 263.552 1.00 69.41 ATOM 1760 CA CYS G 428 119.729 136.521 263.197 1.00 72.69 ATOM 1761 CB CYS G 428 121.237 136.726 263.047 1.00 72.43 ATOM 1762 SG CYS G 428 122.219 136.285 264.496 1.00 64.69 ATOM 1763 C CYS G 428 119.022 137.051 261.948 1.00 76.64 ATOM 1764 O CYS G 428 118.578 138.201 261.921 1.00 78.20 ATOM 1765 N LYS G 429 118.934 136.223 260.913 1.00 80.22 ATOM 1766 CA LYS G 429 118.329 136.650 259.656 1.00 84.07 ATOM 1767 CB LYS G 429 119.025 135.969 258.472 1.00 85.43 ATOM 1768 CG LYS G 429 118.878 136.698 257.142 1.00 87.88 ATOM 1769 CD LYS G 429 119.543 138.066 257.183 1.00 90.50 ATOM 1770 CE LYS G 429 119.373 138.804 255.864 1.00 91.83 ATOM 1771 NZ LYS G 429 120.033 138.087 254.738 1.00 90.48 ATOM 1772 C LYS G 429 116.826 136.362 259.640 1.00 85.52 ATOM 1773 O LYS G 429 116.130 136.685 258.677 1.00 85.93 ATOM 1774 N VAL G 430 116.333 135.761 260.720 1.00 86.23 ATOM 1775 CA VAL G 430 114.931 135.373 260.815 1.00 84.95 ATOM 1776 CB VAL G 430 114.787 133.853 261.069 1.00 85.20 ATOM 1777 CG1 VAL G 430 113.320 133.435 261.063 1.00 88.43 ATOM 1778 CG2 VAL G 430 115.565 133.064 260.027 1.00 84.18 ATOM 1779 C VAL G 430 114.205 136.157 261.911 1.00 84.57 ATOM 1780 O VAL G 430 112.995 136.377 261.829 1.00 85.79 ATOM 1781 N GLY G 431 114.949 136.578 262.931 1.00 83.51 ATOM 1782 CA GLY G 431 114.377 137.340 264.042 1.00 80.76 ATOM 1783 C GLY G 431 113.643 136.479 265.056 1.00 79.30 ATOM 1784 O GLY G 431 112.739 136.949 265.748 1.00 77.09 ATOM 1785 N LYS G 432 114.041 135.214 265.144 1.00 78.54 ATOM 1786 CA LYS G 432 113.396 134.251 266.029 1.00 78.53 ATOM 1787 CB LYS G 432 113.221 132.912 265.301 1.00 79.97 ATOM 1788 CG LYS G 432 112.189 131.967 265.910 1.00 88.19 ATOM 1789 CD LYS G 432 110.838 132.052 265.197 1.00 97.33 ATOM 1790 CE LYS G 432 110.092 133.340 265.523 1.00 101.03 ATOM 1791 NZ LYS G 432 108.767 133.410 264.840 1.00 98.75 ATOM 1792 C LYS G 432 114.212 134.052 267.310 1.00 76.32 ATOM 1793 O LYS G 432 115.413 133.788 267.256 1.00 73.98 ATOM 1794 N MET G 433 113.553 134.186 268.458 1.00 74.04 ATOM 1795 CA MET G 433 114.194 133.959 269.750 1.00 72.02 ATOM 1796 CB MET G 433 113.573 134.850 270.826 1.00 71.91 ATOM 1797 CG MET G 433 114.193 136.229 270.938 1.00 75.09 ATOM 1798 SD MET G 433 113.346 137.270 272.145 1.00 80.56 ATOM 1799 CE MET G 433 111.792 137.572 271.300 1.00 85.21 ATOM 1800 C MET G 433 114.073 132.502 270.172 1.00 68.06 ATOM 1801 O MET G 433 113.121 131.819 269.805 1.00 69.00 ATOM 1802 N MET G 434 115.044 132.036 270.950 1.00 65.48 ATOM 1803 CA MET G 434 115.034 130.670 271.458 1.00 62.50 ATOM 1804 CB MET G 434 116.249 129.899 270.947 1.00 61.04 ATOM 1805 CG MET G 434 116.131 129.521 269.483 1.00 61.46 ATOM 1806 SD MET G 434 117.552 128.623 268.849 1.00 68.17 ATOM 1807 CE MET G 434 118.578 129.958 268.251 1.00 63.93 ATOM 1808 C MET G 434 114.969 130.663 272.980 1.00 58.87 ATOM 1809 O MET G 434 115.717 131.372 273.646 1.00 58.14 ATOM 1810 N TYR G 435 114.058 129.864 273.525 1.00 59.52 ATOM 1811 CA TYR G 435 113.770 129.905 274.952 1.00 59.72 ATOM 1812 CB TYR G 435 112.291 130.211 275.193 1.00 61.23 ATOM 1813 CG TYR G 435 111.835 131.560 274.703 1.00 57.98 ATOM 1814 CD1 TYR G 435 110.831 131.668 273.747 1.00 60.44 ATOM 1815 CE1 TYR G 435 110.400 132.909 273.297 1.00 67.68 ATOM 1816 CZ TYR G 435 110.982 134.057 273.807 1.00 62.94 ATOM 1817 OH TYR G 435 110.566 135.291 273.364 1.00 68.96 ATOM 1818 CE2 TYR G 435 111.981 133.971 274.755 1.00 60.29 ATOM 1819 CD2 TYR G 435 112.401 132.728 275.199 1.00 53.29 ATOM 1820 C TYR G 435 114.114 128.617 275.677 1.00 61.02 ATOM 1821 O TYR G 435 114.331 127.575 275.064 1.00 61.52 ATOM 1822 N ALA G 436 114.155 128.715 277.000 1.00 61.65 ATOM 1823 CA ALA G 436 114.274 127.566 277.872 1.00 61.92 ATOM 1824 CB ALA G 436 115.729 127.176 278.046 1.00 65.04 ATOM 1825 C ALA G 436 113.662 127.943 279.209 1.00 63.18 ATOM 1826 O ALA G 436 113.726 129.101 279.613 1.00 59.47 ATOM 1827 N PRO G 437 113.047 126.969 279.893 1.00 68.05 ATOM 1828 CA PRO G 437 112.585 127.195 281.257 1.00 70.65 ATOM 1829 CB PRO G 437 112.145 125.800 281.709 1.00 71.96 ATOM 1830 CG PRO G 437 111.788 125.092 280.450 1.00 71.56 ATOM 1831 CD PRO G 437 112.749 125.605 279.422 1.00 69.79 ATOM 1832 C PRO G 437 113.746 127.676 282.120 1.00 71.16 ATOM 1833 O PRO G 437 114.872 127.213 281.943 1.00 73.09 ATOM 1834 N PRO G 438 113.483 128.608 283.045 1.00 71.52 ATOM 1835 CA PRO G 438 114.543 129.101 283.911 1.00 74.54 ATOM 1836 CB PRO G 438 114.040 130.489 284.298 1.00 73.30 ATOM 1837 CG PRO G 438 112.553 130.347 284.316 1.00 70.09 ATOM 1838 CD PRO G 438 112.193 129.263 283.324 1.00 71.39 ATOM 1839 C PRO G 438 114.718 128.250 285.168 1.00 78.64 ATOM 1840 O PRO G 438 113.817 127.504 285.549 1.00 79.25 ATOM 1841 N ILE G 439 115.884 128.359 285.794 1.00 83.71 ATOM 1842 CA ILE G 439 116.093 127.821 287.133 1.00 87.96 ATOM 1843 CB ILE G 439 117.548 127.329 287.340 1.00 87.92 ATOM 1844 CG1 ILE G 439 118.551 128.493 287.290 1.00 90.35 ATOM 1845 CD1 ILE G 439 118.540 129.307 286.000 1.00 94.25 ATOM 1846 CG2 ILE G 439 117.898 126.248 286.322 1.00 88.04 ATOM 1847 C ILE G 439 115.743 128.928 288.130 1.00 90.69 ATOM 1848 O ILE G 439 116.597 129.412 288.874 1.00 91.55 ATOM 1849 N SER G 440 114.470 129.316 288.133 1.00 93.48 ATOM 1850 CA SER G 440 114.025 130.546 288.788 1.00 95.61 ATOM 1851 CB SER G 440 112.641 130.961 288.273 1.00 96.06 ATOM 1852 OG SER G 440 111.670 129.965 288.543 1.00 98.80 ATOM 1853 C SER G 440 114.036 130.521 290.317 1.00 96.66 ATOM 1854 O SER G 440 114.958 129.992 290.940 1.00 96.31 ATOM 1855 N GLY G 441 113.002 131.107 290.913 1.00 97.16 ATOM 1856 CA GLY G 441 112.983 131.338 292.350 1.00 97.91 ATOM 1857 C GLY G 441 113.730 132.624 292.640 1.00 97.69 ATOM 1858 O GLY G 441 113.214 133.519 293.309 1.00 98.89 ATOM 1859 N GLN G 442 114.950 132.714 292.117 1.00 95.96 ATOM 1860 CA GLN G 442 115.742 133.932 292.204 1.00 94.29 ATOM 1861 CB GLN G 442 117.191 133.660 291.788 1.00 94.74 ATOM 1862 CG GLN G 442 117.912 132.622 292.639 1.00 95.22 ATOM 1863 CD GLN G 442 118.341 133.158 293.995 1.00 99.61 ATOM 1864 OE1 GLN G 442 118.896 132.427 294.816 1.00 97.05 ATOM 1865 NE2 GLN G 442 118.091 134.441 294.233 1.00 102.54 ATOM 1866 C GLN G 442 115.145 135.017 291.313 1.00 92.44 ATOM 1867 O GLN G 442 115.396 136.206 291.513 1.00 92.72 ATOM 1868 N ILE G 443 114.353 134.599 290.330 1.00 89.08 ATOM 1869 CA ILE G 443 113.752 135.532 289.383 1.00 86.79 ATOM 1870 CB ILE G 443 113.229 134.817 288.111 1.00 87.22 ATOM 1871 CG1 ILE G 443 114.384 134.484 287.161 1.00 89.31 ATOM 1872 CD1 ILE G 443 115.485 133.642 287.767 1.00 94.47 ATOM 1873 CG2 ILE G 443 112.239 135.699 287.372 1.00 85.62 ATOM 1874 C ILE G 443 112.635 136.354 290.027 1.00 83.95 ATOM 1875 O ILE G 443 111.485 135.922 290.098 1.00 82.73 ATOM 1876 N ARG G 444 112.998 137.534 290.516 1.00 81.65 ATOM 1877 CA ARG G 444 112.023 138.512 290.975 1.00 80.43 ATOM 1878 CB ARG G 444 112.297 138.937 292.418 1.00 80.82 ATOM 1879 CG ARG G 444 111.341 138.344 293.438 1.00 83.23 ATOM 1880 CD ARG G 444 111.898 137.094 294.085 1.00 90.19 ATOM 1881 NE ARG G 444 111.046 136.648 295.182 1.00 97.36 ATOM 1882 CZ ARG G 444 111.495 136.069 296.291 1.00 105.27 ATOM 1883 NH1 ARG G 444 110.644 135.697 297.237 1.00 109.62 ATOM 1884 NH2 ARG G 444 112.796 135.870 296.460 1.00 109.75 ATOM 1885 C ARG G 444 112.057 139.729 290.064 1.00 79.03 ATOM 1886 O ARG G 444 113.106 140.077 289.520 1.00 77.75 ATOM 1887 N CYS G 445 110.906 140.373 289.899 1.00 78.84 ATOM 1888 CA CYS G 445 110.813 141.556 289.054 1.00 76.09 ATOM 1889 CB CYS G 445 110.603 141.161 287.593 1.00 77.04 ATOM 1890 SG CYS G 445 110.584 142.564 286.452 1.00 85.51 ATOM 1891 C CYS G 445 109.696 142.485 289.508 1.00 72.72 ATOM 1892 O CYS G 445 108.536 142.083 289.601 1.00 70.96 ATOM 1893 N SER G 446 110.056 143.730 289.791 1.00 70.26 ATOM 1894 CA SER G 446 109.084 144.732 290.186 1.00 70.05 ATOM 1895 CB SER G 446 109.278 145.134 291.647 1.00 69.76 ATOM 1896 OG SER G 446 110.451 145.913 291.806 1.00 78.13 ATOM 1897 C SER G 446 109.232 145.946 289.287 1.00 69.38 ATOM 1898 O SER G 446 110.312 146.529 289.188 1.00 69.42 ATOM 1899 N SER G 447 108.141 146.317 288.630 1.00 66.95 ATOM 1900 CA SER G 447 108.153 147.437 287.709 1.00 66.61 ATOM 1901 CB SER G 447 107.977 146.947 286.269 1.00 64.24 ATOM 1902 OG SER G 447 108.796 145.820 286.003 1.00 62.54 ATOM 1903 C SER G 447 107.040 148.415 288.047 1.00 66.43 ATOM 1904 O SER G 447 106.238 148.178 288.951 1.00 66.80 ATOM 1905 N ASN G 448 107.011 149.521 287.316 1.00 64.62 ATOM 1906 CA ASN G 448 105.909 150.457 287.386 1.00 63.48 ATOM 1907 CB ASN G 448 106.425 151.879 287.589 1.00 65.97 ATOM 1908 CG ASN G 448 106.651 152.218 289.043 1.00 74.03 ATOM 1909 OD1 ASN G 448 106.207 151.498 289.938 1.00 76.80 ATOM 1910 ND2 ASN G 448 107.337 153.331 289.289 1.00 90.49 ATOM 1911 C ASN G 448 105.118 150.403 286.094 1.00 62.86 ATOM 1912 O ASN G 448 105.673 150.620 285.019 1.00 61.49 ATOM 1913 N ILE G 449 103.831 150.092 286.190 1.00 61.54 ATOM 1914 CA ILE G 449 102.934 150.323 285.071 1.00 60.13 ATOM 1915 CB ILE G 449 101.546 149.703 285.312 1.00 58.54 ATOM 1916 CG1 ILE G 449 101.675 148.193 285.538 1.00 64.29 ATOM 1917 CD1 ILE G 449 100.372 147.497 285.870 1.00 61.24 ATOM 1918 CG2 ILE G 449 100.606 150.006 284.145 1.00 61.01 ATOM 1919 C ILE G 449 102.829 151.839 284.943 1.00 58.48 ATOM 1920 O ILE G 449 102.401 152.513 285.881 1.00 57.80 ATOM 1921 N THR G 450 103.263 152.371 283.803 1.00 57.73 ATOM 1922 CA THR G 450 103.258 153.820 283.573 1.00 59.53 ATOM 1923 CB THR G 450 104.662 154.333 283.207 1.00 55.72 ATOM 1924 OG1 THR G 450 105.199 153.530 282.148 1.00 59.50 ATOM 1925 CG2 THR G 450 105.592 154.263 284.409 1.00 57.57 ATOM 1926 C THR G 450 102.286 154.212 282.455 1.00 60.99 ATOM 1927 O THR G 450 102.008 155.393 282.238 1.00 62.34 ATOM 1928 N GLY G 451 101.778 153.207 281.750 1.00 61.05 ATOM 1929 CA GLY G 451 100.859 153.421 280.635 1.00 63.51 ATOM 1930 C GLY G 451 100.467 152.097 280.011 1.00 63.05 ATOM 1931 O GLY G 451 100.865 151.042 280.500 1.00 66.04 ATOM 1932 N LEU G 452 99.682 152.139 278.938 1.00 66.57 ATOM 1933 CA LEU G 452 99.281 150.911 278.257 1.00 67.38 ATOM 1934 CB LEU G 452 98.140 150.205 278.992 1.00 69.48 ATOM 1935 CG LEU G 452 96.895 151.011 279.346 1.00 72.28 ATOM 1936 CD1 LEU G 452 95.642 150.163 279.191 1.00 65.14 ATOM 1937 CD2 LEU G 452 97.026 151.544 280.762 1.00 78.48 ATOM 1938 C LEU G 452 98.893 151.115 276.804 1.00 67.07 ATOM 1939 O LEU G 452 98.631 152.233 276.361 1.00 71.14 ATOM 1940 N LEU G 453 98.860 150.010 276.071 1.00 65.09 ATOM 1941 CA LEU G 453 98.462 150.023 274.677 1.00 62.11 ATOM 1942 CB LEU G 453 99.408 149.156 273.851 1.00 62.89 ATOM 1943 CG LEU G 453 100.887 149.540 273.851 1.00 59.38 ATOM 1944 CD1 LEU G 453 101.693 148.496 273.113 1.00 51.51 ATOM 1945 CD2 LEU G 453 101.086 150.909 273.228 1.00 52.92 ATOM 1946 C LEU G 453 97.056 149.468 274.564 1.00 63.78 ATOM 1947 O LEU G 453 96.738 148.436 275.163 1.00 58.80 ATOM 1948 N LEU G 454 96.214 150.159 273.805 1.00 61.47 ATOM 1949 CA LEU G 454 94.866 149.685 273.541 1.00 62.05 ATOM 1950 CB LEU G 454 93.834 150.541 274.281 1.00 58.73 ATOM 1951 CG LEU G 454 93.868 150.509 275.812 1.00 64.94 ATOM 1952 CD1 LEU G 454 92.983 151.593 276.386 1.00 60.69 ATOM 1953 CD2 LEU G 454 93.470 149.130 276.352 1.00 49.13 ATOM 1954 C LEU G 454 94.579 149.730 272.054 1.00 63.55 ATOM 1955 O LEU G 454 95.129 150.563 271.333 1.00 63.19 ATOM 1956 N THR G 455 93.729 148.816 271.597 1.00 62.38 ATOM 1957 CA THR G 455 93.096 148.956 270.295 1.00 64.23 ATOM 1958 CB THR G 455 93.518 147.864 269.293 1.00 64.42 ATOM 1959 OG1 THR G 455 92.950 146.609 269.683 1.00 67.24 ATOM 1960 CG2 THR G 455 95.035 147.743 269.223 1.00 66.62 ATOM 1961 C THR G 455 91.595 148.887 270.501 1.00 62.32 ATOM 1962 O THR G 455 91.105 148.153 271.362 1.00 64.97 ATOM 1963 N ARG G 456 90.872 149.660 269.704 1.00 61.50 ATOM 1964 CA ARG G 456 89.430 149.763 269.815 1.00 58.53 ATOM 1965 CB ARG G 456 89.030 151.228 269.617 1.00 58.26 ATOM 1966 CG ARG G 456 87.548 151.521 269.749 1.00 59.41 ATOM 1967 CD ARG G 456 87.304 153.023 269.709 1.00 62.45 ATOM 1968 NE ARG G 456 87.773 153.612 268.460 1.00 63.68 ATOM 1969 CZ ARG G 456 87.015 153.753 267.378 1.00 67.17 ATOM 1970 NH1 ARG G 456 85.754 153.351 267.397 1.00 68.51 ATOM 1971 NH2 ARG G 456 87.516 154.298 266.278 1.00 60.97 ATOM 1972 C ARG G 456 88.755 148.873 268.774 1.00 58.22 ATOM 1973 O ARG G 456 89.164 148.860 267.612 1.00 63.04 ATOM 1974 N ASP G 457 87.728 148.130 269.188 1.00 59.79 ATOM 1975 CA ASP G 457 86.981 147.256 268.272 1.00 57.43 ATOM 1976 CB ASP G 457 85.908 146.458 269.023 1.00 56.99 ATOM 1977 CG ASP G 457 86.462 145.234 269.729 1.00 66.50 ATOM 1978 OD1 ASP G 457 87.692 145.144 269.937 1.00 68.77 ATOM 1979 OD2 ASP G 457 85.650 144.359 270.088 1.00 73.47 ATOM 1980 C ASP G 457 86.298 148.032 267.153 1.00 61.42 ATOM 1981 O ASP G 457 85.754 149.115 267.378 1.00 63.64 ATOM 1982 N GLY G 458 86.295 147.453 265.954 1.00 62.51 ATOM 1983 CA GLY G 458 85.625 148.052 264.809 1.00 61.83 ATOM 1984 C GLY G 458 84.303 147.395 264.435 1.00 68.26 ATOM 1985 O GLY G 458 83.600 147.871 263.539 1.00 68.39 ATOM 1986 N GLY G 459 83.950 146.309 265.118 1.00 67.87 ATOM 1987 CA GLY G 459 82.721 145.584 264.784 1.00 73.35 ATOM 1988 C GLY G 459 81.552 145.863 265.714 1.00 73.69 ATOM 1989 O GLY G 459 80.457 145.329 265.524 1.00 72.08 ATOM 1990 N ASN G 460 81.796 146.705 266.717 1.00 73.79 ATOM 1991 CA ASN G 460 80.819 147.022 267.758 1.00 67.44 ATOM 1992 CB ASN G 460 81.459 147.956 268.791 1.00 67.48 ATOM 1993 CG ASN G 460 80.537 148.268 269.954 1.00 64.90 ATOM 1994 OD1 ASN G 460 79.463 147.675 270.096 1.00 55.56 ATOM 1995 ND2 ASN G 460 80.954 149.202 270.797 1.00 60.87 ATOM 1996 C ASN G 460 79.527 147.638 267.224 1.00 67.67 ATOM 1997 O ASN G 460 79.531 148.767 266.737 1.00 68.38 ATOM 1998 N SER G 461 78.426 146.894 267.338 1.00 66.00 ATOM 1999 CA SER G 461 77.118 147.333 266.847 1.00 64.96 ATOM 2000 CB SER G 461 76.207 146.131 266.572 1.00 65.12 ATOM 2001 OG SER G 461 76.729 145.305 265.547 1.00 74.90 ATOM 2002 C SER G 461 76.404 148.275 267.810 1.00 64.11 ATOM 2003 O SER G 461 75.278 148.700 267.541 1.00 58.71 ATOM 2004 N ASN G 462 77.044 148.584 268.934 1.00 62.43 ATOM 2005 CA ASN G 462 76.460 149.489 269.922 1.00 63.37 ATOM 2006 CB ASN G 462 76.729 148.994 271.349 1.00 62.00 ATOM 2007 CG ASN G 462 75.874 149.708 272.393 1.00 53.01 ATOM 2008 OD1 ASN G 462 75.091 150.599 272.072 1.00 53.91 ATOM 2009 ND2 ASN G 462 76.025 149.308 273.650 1.00 49.31 ATOM 2010 C ASN G 462 76.991 150.904 269.753 1.00 64.80 ATOM 2011 O ASN G 462 78.179 151.162 269.957 1.00 65.33 ATOM 2012 N ASN G 463 76.103 151.817 269.377 1.00 64.50 ATOM 2013 CA ASN G 463 76.478 153.206 269.161 1.00 69.19 ATOM 2014 CB ASN G 463 75.459 153.891 268.248 1.00 70.16 ATOM 2015 CG ASN G 463 75.367 153.234 266.883 1.00 79.27 ATOM 2016 OD1 ASN G 463 76.374 152.801 266.321 1.00 82.43 ATOM 2017 ND2 ASN G 463 74.157 153.158 266.343 1.00 93.34 ATOM 2018 C ASN G 463 76.601 153.966 270.476 1.00 68.19 ATOM 2019 O ASN G 463 76.807 155.178 270.490 1.00 70.78 ATOM 2020 N GLU G 464 76.472 153.242 271.580 1.00 64.52 ATOM 2021 CA GLU G 464 76.499 153.848 272.897 1.00 62.61 ATOM 2022 CB GLU G 464 75.181 153.574 273.624 1.00 65.07 ATOM 2023 CG GLU G 464 74.008 154.400 273.097 1.00 69.54 ATOM 2024 CD GLU G 464 72.724 153.593 272.978 1.00 83.98 ATOM 2025 OE1 GLU G 464 71.657 154.109 273.377 1.00 88.52 ATOM 2026 OE2 GLU G 464 72.781 152.445 272.483 1.00 81.48 ATOM 2027 C GLU G 464 77.676 153.321 273.698 1.00 61.60 ATOM 2028 O GLU G 464 77.809 153.605 274.885 1.00 62.84 ATOM 2029 N SER G 465 78.535 152.552 273.042 1.00 60.26 ATOM 2030 CA SER G 465 79.693 151.991 273.716 1.00 59.73 ATOM 2031 CB SER G 465 79.392 150.580 274.227 1.00 61.66 ATOM 2032 OG SER G 465 79.683 149.607 273.235 1.00 56.72 ATOM 2033 C SER G 465 80.903 151.938 272.805 1.00 58.63 ATOM 2034 O SER G 465 80.779 151.990 271.582 1.00 58.39 ATOM 2035 N GLU G 466 82.072 151.838 273.425 1.00 61.48 ATOM 2036 CA GLU G 466 83.318 151.572 272.728 1.00 61.53 ATOM 2037 CB GLU G 466 84.207 152.817 272.691 1.00 65.49 ATOM 2038 CG GLU G 466 83.636 153.998 271.909 1.00 63.36 ATOM 2039 CD GLU G 466 83.426 153.700 270.427 1.00 65.00 ATOM 2040 OE1 GLU G 466 82.717 154.484 269.759 1.00 71.68 ATOM 2041 OE2 GLU G 466 83.964 152.688 269.928 1.00 65.76 ATOM 2042 C GLU G 466 84.027 150.449 273.461 1.00 60.19 ATOM 2043 O GLU G 466 84.058 150.422 274.689 1.00 59.78 ATOM 2044 N ILE G 467 84.584 149.510 272.706 1.00 61.27 ATOM 2045 CA ILE G 467 85.276 148.374 273.292 1.00 58.52 ATOM 2046 CB ILE G 467 84.781 147.043 272.697 1.00 61.18 ATOM 2047 CG1 ILE G 467 83.308 146.812 273.049 1.00 56.18 ATOM 2048 CD1 ILE G 467 82.729 145.561 272.427 1.00 55.77 ATOM 2049 CG2 ILE G 467 85.643 145.884 273.179 1.00 54.60 ATOM 2050 C ILE G 467 86.767 148.496 273.046 1.00 61.26 ATOM 2051 O ILE G 467 87.202 148.682 271.911 1.00 63.07 ATOM 2052 N PHE G 468 87.546 148.381 274.115 1.00 60.15 ATOM 2053 CA PHE G 468 88.991 148.463 274.017 1.00 60.12 ATOM 2054 CB PHE G 468 89.502 149.691 274.779 1.00 54.48 ATOM 2055 CG PHE G 468 88.867 150.978 274.326 1.00 59.49 ATOM 2056 CD1 PHE G 468 87.626 151.361 274.810 1.00 54.32 ATOM 2057 CE1 PHE G 468 87.033 152.533 274.388 1.00 63.91 ATOM 2058 CZ PHE G 468 87.677 153.340 273.468 1.00 62.91 ATOM 2059 CE2 PHE G 468 88.908 152.966 272.971 1.00 64.72 ATOM 2060 CD2 PHE G 468 89.497 151.791 273.397 1.00 55.45 ATOM 2061 C PHE G 468 89.643 147.185 274.525 1.00 60.56 ATOM 2062 O PHE G 468 89.202 146.602 275.515 1.00 62.20 ATOM 2063 N ARG G 469 90.684 146.746 273.827 1.00 57.59 ATOM 2064 CA ARG G 469 91.420 145.550 274.219 1.00 61.83 ATOM 2065 CB ARG G 469 91.238 144.439 273.183 1.00 56.39 ATOM 2066 CG ARG G 469 89.784 144.168 272.843 1.00 64.86 ATOM 2067 CD ARG G 469 89.619 142.995 271.887 1.00 60.37 ATOM 2068 NE ARG G 469 88.218 142.824 271.524 1.00 61.46 ATOM 2069 CZ ARG G 469 87.436 141.848 271.970 1.00 61.40 ATOM 2070 NH1 ARG G 469 87.918 140.922 272.789 1.00 65.54 ATOM 2071 NH2 ARG G 469 86.171 141.789 271.581 1.00 63.89 ATOM 2072 C ARG G 469 92.893 145.901 274.383 1.00 61.58 ATOM 2073 O ARG G 469 93.394 146.810 273.715 1.00 63.69 ATOM 2074 N PRO G 470 93.592 145.192 275.281 1.00 61.41 ATOM 2075 CA PRO G 470 94.994 145.497 275.541 1.00 60.93 ATOM 2076 CB PRO G 470 95.293 144.677 276.792 1.00 62.38 ATOM 2077 CG PRO G 470 94.374 143.497 276.674 1.00 61.54 ATOM 2078 CD PRO G 470 93.111 144.064 276.098 1.00 59.49 ATOM 2079 C PRO G 470 95.869 145.034 274.384 1.00 60.81 ATOM 2080 O PRO G 470 95.575 144.020 273.751 1.00 66.76 ATOM 2081 N GLY G 471 96.931 145.781 274.109 1.00 63.26 ATOM 2082 CA GLY G 471 97.840 145.448 273.025 1.00 63.87 ATOM 2083 C GLY G 471 97.733 146.454 271.904 1.00 67.30 ATOM 2084 O GLY G 471 96.722 147.142 271.780 1.00 72.53 ATOM 2085 N GLY G 472 98.790 146.555 271.102 1.00 68.58 ATOM 2086 CA GLY G 472 98.803 147.425 269.934 1.00 65.28 ATOM 2087 C GLY G 472 98.621 146.613 268.668 1.00 67.34 ATOM 2088 O GLY G 472 98.435 145.398 268.732 1.00 69.97 ATOM 2089 N GLY G 473 98.662 147.279 267.517 1.00 64.21 ATOM 2090 CA GLY G 473 98.562 146.595 266.226 1.00 59.04 ATOM 2091 C GLY G 473 99.930 146.216 265.687 1.00 61.91 ATOM 2092 O GLY G 473 100.043 145.569 264.642 1.00 59.36 ATOM 2093 N ASP G 474 100.976 146.635 266.396 1.00 61.57 ATOM 2094 CA ASP G 474 102.348 146.338 265.994 1.00 58.42 ATOM 2095 CB ASP G 474 102.944 147.485 265.168 1.00 53.77 ATOM 2096 CG ASP G 474 104.356 147.179 264.684 1.00 64.01 ATOM 2097 OD1 ASP G 474 105.323 147.788 265.201 1.00 63.69 ATOM 2098 OD2 ASP G 474 104.505 146.303 263.806 1.00 61.13 ATOM 2099 C ASP G 474 103.226 146.056 267.208 1.00 61.44 ATOM 2100 O ASP G 474 103.020 146.618 268.292 1.00 59.39 ATOM 2101 N MET G 475 104.213 145.187 267.019 1.00 62.96 ATOM 2102 CA MET G 475 105.105 144.802 268.103 1.00 64.26 ATOM 2103 CB MET G 475 106.076 143.716 267.635 1.00 66.51 ATOM 2104 CG MET G 475 107.104 143.316 268.677 1.00 66.56 ATOM 2105 SD MET G 475 107.683 141.631 268.455 1.00 73.31 ATOM 2106 CE MET G 475 109.187 141.649 269.434 1.00 77.19 ATOM 2107 C MET G 475 105.870 145.985 268.694 1.00 62.19 ATOM 2108 O MET G 475 106.072 146.049 269.906 1.00 61.48 ATOM 2109 N ARG G 476 106.277 146.928 267.846 1.00 60.57 ATOM 2110 CA ARG G 476 107.096 148.058 268.294 1.00 59.50 ATOM 2111 CB ARG G 476 108.007 148.559 267.166 1.00 60.87 ATOM 2112 CG ARG G 476 108.962 147.519 266.620 1.00 57.37 ATOM 2113 CD ARG G 476 109.478 146.643 267.731 1.00 63.48 ATOM 2114 NE ARG G 476 110.482 145.703 267.257 1.00 68.36 ATOM 2115 CZ ARG G 476 111.024 144.753 268.010 1.00 66.33 ATOM 2116 NH1 ARG G 476 111.935 143.939 267.494 1.00 48.43 ATOM 2117 NH2 ARG G 476 110.652 144.617 269.277 1.00 63.64 ATOM 2118 C ARG G 476 106.284 149.232 268.843 1.00 60.59 ATOM 2119 O ARG G 476 106.819 150.324 269.022 1.00 62.57 ATOM 2120 N ASP G 477 105.003 149.016 269.114 1.00 52.38 ATOM 2121 CA ASP G 477 104.175 150.086 269.657 1.00 57.46 ATOM 2122 CB ASP G 477 102.705 149.673 269.718 1.00 58.49 ATOM 2123 CG ASP G 477 102.021 149.761 268.362 1.00 56.49 ATOM 2124 OD1 ASP G 477 100.920 149.192 268.209 1.00 58.78 ATOM 2125 OD2 ASP G 477 102.585 150.400 267.448 1.00 61.06 ATOM 2126 C ASP G 477 104.660 150.575 271.021 1.00 62.24 ATOM 2127 O ASP G 477 104.510 151.758 271.343 1.00 62.77 ATOM 2128 N ASN G 478 105.249 149.678 271.814 1.00 61.83 ATOM 2129 CA ASN G 478 105.825 150.080 273.096 1.00 61.48 ATOM 2130 CB ASN G 478 106.279 148.872 273.936 1.00 63.15 ATOM 2131 CG ASN G 478 107.500 148.154 273.358 1.00 62.95 ATOM 2132 OD1 ASN G 478 108.500 147.959 274.050 1.00 62.40 ATOM 2133 ND2 ASN G 478 107.410 147.736 272.102 1.00 49.20 ATOM 2134 C ASN G 478 106.955 151.081 272.896 1.00 62.06 ATOM 2135 O ASN G 478 107.126 152.010 273.688 1.00 65.07 ATOM 2136 N TRP G 479 107.713 150.897 271.820 1.00 59.76 ATOM 2137 CA TRP G 479 108.746 151.848 271.432 1.00 55.58 ATOM 2138 CB TRP G 479 109.508 151.314 270.222 1.00 52.69 ATOM 2139 CG TRP G 479 110.285 150.063 270.503 1.00 58.74 ATOM 2140 CD1 TRP G 479 110.229 149.294 271.632 1.00 54.03 ATOM 2141 NE1 TRP G 479 111.078 148.224 271.519 1.00 51.36 ATOM 2142 CE2 TRP G 479 111.697 148.276 270.297 1.00 55.29 ATOM 2143 CD2 TRP G 479 111.221 149.422 269.629 1.00 47.68 ATOM 2144 CE3 TRP G 479 111.704 149.708 268.349 1.00 49.22 ATOM 2145 CZ3 TRP G 479 112.634 148.852 267.786 1.00 52.69 ATOM 2146 CH2 TRP G 479 113.088 147.721 268.476 1.00 55.11 ATOM 2147 CZ2 TRP G 479 112.633 147.417 269.729 1.00 47.47 ATOM 2148 C TRP G 479 108.111 153.195 271.092 1.00 57.38 ATOM 2149 O TRP G 479 108.573 154.245 271.543 1.00 57.26 ATOM 2150 N ARG G 480 107.037 153.153 270.306 1.00 56.68 ATOM 2151 CA ARG G 480 106.358 154.365 269.840 1.00 58.55 ATOM 2152 CB ARG G 480 105.228 154.008 268.869 1.00 55.11 ATOM 2153 CG ARG G 480 105.708 153.387 267.567 1.00 49.33 ATOM 2154 CD ARG G 480 104.569 153.173 266.577 1.00 55.62 ATOM 2155 NE ARG G 480 105.072 152.654 265.309 1.00 60.50 ATOM 2156 CZ ARG G 480 105.295 151.366 265.067 1.00 62.97 ATOM 2157 NH1 ARG G 480 105.765 150.983 263.888 1.00 64.23 ATOM 2158 NH2 ARG G 480 105.048 150.460 266.003 1.00 52.83 ATOM 2159 C ARG G 480 105.815 155.217 270.984 1.00 58.78 ATOM 2160 O ARG G 480 105.715 156.437 270.863 1.00 62.54 ATOM 2161 N SER G 481 105.468 154.569 272.091 1.00 60.72 ATOM 2162 CA SER G 481 104.922 155.262 273.248 1.00 62.84 ATOM 2163 CB SER G 481 104.469 154.253 274.300 1.00 63.66 ATOM 2164 OG SER G 481 105.569 153.775 275.052 1.00 63.38 ATOM 2165 C SER G 481 105.956 156.196 273.860 1.00 65.25 ATOM 2166 O SER G 481 105.621 157.099 274.624 1.00 67.47 ATOM 2167 N GLU G 482 107.216 155.977 273.512 1.00 66.51 ATOM 2168 CA GLU G 482 108.308 156.717 274.123 1.00 71.38 ATOM 2169 CB GLU G 482 109.298 155.732 274.757 1.00 71.76 ATOM 2170 CG GLU G 482 109.991 156.244 276.009 1.00 86.77 ATOM 2171 CD GLU G 482 109.026 156.529 277.149 1.00 94.64 ATOM 2172 OE1 GLU G 482 108.185 155.654 277.449 1.00 91.76 ATOM 2173 OE2 GLU G 482 109.118 157.623 277.749 1.00 90.10 ATOM 2174 C GLU G 482 109.016 157.618 273.108 1.00 68.49 ATOM 2175 O GLU G 482 109.909 158.385 273.465 1.00 71.33 ATOM 2176 N LEU G 483 108.597 157.539 271.847 1.00 68.25 ATOM 2177 CA LEU G 483 109.307 158.213 270.759 1.00 67.59 ATOM 2178 CB LEU G 483 109.734 157.191 269.702 1.00 64.18 ATOM 2179 CG LEU G 483 110.846 156.205 270.071 1.00 67.01 ATOM 2180 CD1 LEU G 483 110.877 155.052 269.085 1.00 62.12 ATOM 2181 CD2 LEU G 483 112.205 156.900 270.138 1.00 56.43 ATOM 2182 C LEU G 483 108.522 159.338 270.081 1.00 68.52 ATOM 2183 O LEU G 483 108.913 159.806 269.013 1.00 70.55 ATOM 2184 N TYR G 484 107.429 159.779 270.698 1.00 70.47 ATOM 2185 CA TYR G 484 106.529 160.750 270.063 1.00 69.79 ATOM 2186 CB TYR G 484 105.133 160.697 270.700 1.00 70.27 ATOM 2187 CG TYR G 484 105.093 161.151 272.144 1.00 74.53 ATOM 2188 CD1 TYR G 484 104.846 162.479 272.468 1.00 73.05 ATOM 2189 CE1 TYR G 484 104.813 162.902 273.785 1.00 78.20 ATOM 2190 CZ TYR G 484 105.021 161.991 274.799 1.00 78.35 ATOM 2191 OH TYR G 484 104.984 162.414 276.109 1.00 80.42 ATOM 2192 CE2 TYR G 484 105.268 160.664 274.507 1.00 76.46 ATOM 2193 CD2 TYR G 484 105.302 160.251 273.185 1.00 76.77 ATOM 2194 C TYR G 484 107.053 162.190 270.058 1.00 67.11 ATOM 2195 O TYR G 484 106.576 163.028 269.290 1.00 65.91 ATOM 2196 N LYS G 485 108.026 162.481 270.913 1.00 65.99 ATOM 2197 CA LYS G 485 108.571 163.835 270.990 1.00 67.01 ATOM 2198 CB LYS G 485 108.776 164.264 272.448 1.00 67.55 ATOM 2199 CG LYS G 485 109.245 163.158 273.378 1.00 76.82 ATOM 2200 CD LYS G 485 109.312 163.655 274.814 1.00 88.24 ATOM 2201 CE LYS G 485 109.563 162.515 275.790 1.00 96.31 ATOM 2202 NZ LYS G 485 109.692 163.009 277.191 1.00 98.22 ATOM 2203 C LYS G 485 109.856 164.027 270.182 1.00 64.40 ATOM 2204 O LYS G 485 110.568 165.011 270.369 1.00 63.54 ATOM 2205 N TYR G 486 110.144 163.095 269.277 1.00 63.37 ATOM 2206 CA TYR G 486 111.346 163.188 268.450 1.00 62.01 ATOM 2207 CB TYR G 486 112.269 161.991 268.685 1.00 62.23 ATOM 2208 CG TYR G 486 112.726 161.803 270.112 1.00 58.07 ATOM 2209 CD1 TYR G 486 113.746 162.579 270.646 1.00 55.20 ATOM 2210 CE1 TYR G 486 114.170 162.397 271.950 1.00 60.40 ATOM 2211 CZ TYR G 486 113.572 161.426 272.730 1.00 58.38 ATOM 2212 OH TYR G 486 113.981 161.230 274.029 1.00 62.60 ATOM 2213 CE2 TYR G 486 112.566 160.644 272.216 1.00 54.32 ATOM 2214 CD2 TYR G 486 112.151 160.833 270.917 1.00 52.13 ATOM 2215 C TYR G 486 111.041 163.303 266.958 1.00 60.93 ATOM 2216 O TYR G 486 109.991 162.866 266.487 1.00 62.10 ATOM 2217 N LYS G 487 111.987 163.878 266.223 1.00 60.90 ATOM 2218 CA LYS G 487 111.867 164.069 264.784 1.00 61.65 ATOM 2219 CB LYS G 487 111.048 165.328 264.487 1.00 62.66 ATOM 2220 CG LYS G 487 111.201 165.872 263.070 1.00 62.15 ATOM 2221 CD LYS G 487 110.537 167.237 262.928 1.00 61.61 ATOM 2222 CE LYS G 487 110.606 167.741 261.493 1.00 67.47 ATOM 2223 NZ LYS G 487 110.240 169.182 261.378 1.00 62.32 ATOM 2224 C LYS G 487 113.259 164.205 264.179 1.00 61.25 ATOM 2225 O LYS G 487 114.057 165.025 264.627 1.00 57.91 ATOM 2226 N VAL G 488 113.547 163.391 263.167 1.00 62.69 ATOM 2227 CA VAL G 488 114.849 163.407 262.503 1.00 63.92 ATOM 2228 CB VAL G 488 115.222 162.007 261.962 1.00 64.63 ATOM 2229 CG1 VAL G 488 116.673 161.979 261.493 1.00 62.43 ATOM 2230 CG2 VAL G 488 114.988 160.949 263.025 1.00 61.40 ATOM 2231 C VAL G 488 114.877 164.414 261.352 1.00 63.73 ATOM 2232 O VAL G 488 113.986 164.419 260.503 1.00 64.94 ATOM 2233 N VAL G 489 115.898 165.265 261.331 1.00 64.02 ATOM 2234 CA VAL G 489 116.034 166.272 260.278 1.00 65.06 ATOM 2235 CB VAL G 489 115.581 167.671 260.759 1.00 65.13 ATOM 2236 CG1 VAL G 489 114.143 167.623 261.249 1.00 65.33 ATOM 2237 CG2 VAL G 489 116.507 168.195 261.850 1.00 61.42 ATOM 2238 C VAL G 489 117.462 166.365 259.737 1.00 65.93 ATOM 2239 O VAL G 489 118.398 165.829 260.328 1.00 63.26 ATOM 2240 N LYS G 490 117.612 167.053 258.606 1.00 68.03 ATOM 2241 CA LYS G 490 118.917 167.284 257.993 1.00 69.65 ATOM 2242 CB LYS G 490 118.761 167.593 256.501 1.00 70.26 ATOM 2243 CG LYS G 490 118.098 166.496 255.681 1.00 71.91 ATOM 2244 CD LYS G 490 117.833 166.941 254.242 1.00 68.66 ATOM 2245 CE LYS G 490 119.124 167.173 253.459 1.00 70.29 ATOM 2246 NZ LYS G 490 119.670 168.555 253.620 1.00 64.36 ATOM 2247 C LYS G 490 119.628 168.452 258.666 1.00 70.43 ATOM 2248 O LYS G 490 118.992 169.430 259.060 1.00 70.15 ATOM 2249 N ILE G 491 120.947 168.350 258.793 1.00 71.14 ATOM 2250 CA ILE G 491 121.739 169.460 259.306 1.00 73.03 ATOM 2251 CB ILE G 491 123.216 169.063 259.514 1.00 72.87 ATOM 2252 CG1 ILE G 491 123.349 168.117 260.710 1.00 74.69 ATOM 2253 CD1 ILE G 491 122.926 168.727 262.031 1.00 74.39 ATOM 2254 CG2 ILE G 491 124.084 170.297 259.725 1.00 72.87 ATOM 2255 C ILE G 491 121.641 170.631 258.336 1.00 75.06 ATOM 2256 O ILE G 491 122.037 170.522 257.174 1.00 76.22 ATOM 2257 N GLU G 492 121.094 171.744 258.816 1.00 76.21 ATOM 2258 CA GLU G 492 120.876 172.922 257.983 1.00 77.33 ATOM 2259 CB GLU G 492 119.958 173.916 258.701 1.00 77.92 ATOM 2260 CG GLU G 492 119.283 174.927 257.784 1.00 78.10 ATOM 2261 CD GLU G 492 118.074 174.354 257.064 1.00 79.21 ATOM 2262 OE1 GLU G 492 117.565 175.022 256.138 1.00 79.62 ATOM 2263 OE2 GLU G 492 117.631 173.241 257.423 1.00 70.96 ATOM 2264 C GLU G 492 122.194 173.598 257.609 1.00 77.61 ATOM 2265 O GLU G 492 123.085 173.765 258.442 1.00 77.51 ATOM 2266 OXT GLU G 492 122.402 173.991 256.461 1.00 78.04 ATOM 2267 C1 NAG G 734 96.821 167.516 269.497 1.00 121.31 ATOM 2268 C2 NAG G 734 96.238 168.237 268.281 1.00 131.46 ATOM 2269 N2 NAG G 734 97.304 168.819 267.483 1.00 135.44 ATOM 2270 C7 NAG G 734 97.137 169.182 266.211 1.00 137.22 ATOM 2271 O7 NAG G 734 97.498 170.277 265.779 1.00 134.28 ATOM 2272 C8 NAG G 734 96.479 168.186 265.299 1.00 136.15 ATOM 2273 C3 NAG G 734 95.238 169.316 268.699 1.00 131.64 ATOM 2274 O3 NAG G 734 94.515 169.757 267.570 1.00 128.15 ATOM 2275 C4 NAG G 734 94.260 168.798 269.751 1.00 131.03 ATOM 2276 O4 NAG G 734 93.551 169.883 270.311 1.00 129.65 ATOM 2277 C5 NAG G 734 94.988 168.035 270.854 1.00 128.58 ATOM 2278 C6 NAG G 734 94.005 167.428 271.849 1.00 128.98 ATOM 2279 O6 NAG G 734 94.421 166.123 272.180 1.00 128.54 ATOM 2280 O5 NAG G 734 95.763 167.006 270.279 1.00 124.84 ATOM 2281 C1 NAG G 741 111.230 173.879 278.108 1.00 125.89 ATOM 2282 C2 NAG G 741 111.834 173.321 279.397 1.00 134.78 ATOM 2283 N2 NAG G 741 112.630 172.135 279.129 1.00 134.84 ATOM 2284 C7 NAG G 741 113.699 171.828 279.863 1.00 134.16 ATOM 2285 O7 NAG G 741 114.685 172.559 279.953 1.00 134.06 ATOM 2286 C8 NAG G 741 113.656 170.520 280.598 1.00 130.23 ATOM 2287 C3 NAG G 741 110.732 173.021 280.411 1.00 135.42 ATOM 2288 O3 NAG G 741 111.296 172.660 281.654 1.00 134.08 ATOM 2289 C4 NAG G 741 109.825 174.235 280.590 1.00 136.01 ATOM 2290 O4 NAG G 741 108.702 173.875 281.366 1.00 136.57 ATOM 2291 C5 NAG G 741 109.367 174.782 279.238 1.00 136.00 ATOM 2292 C6 NAG G 741 108.557 176.062 279.411 1.00 138.38 ATOM 2293 O6 NAG G 741 107.779 176.292 278.257 1.00 141.28 ATOM 2294 O5 NAG G 741 110.486 173.043 278.412 1.00 133.24 ATOM 2295 C1 NAG G 762 111.547 148.597 286.249 1.00 88.10 ATOM 2296 C2 NAG G 762 112.176 147.316 285.696 1.00 91.32 ATOM 2297 N2 NAG G 762 111.174 146.517 285.011 1.00 76.31 ATOM 2298 C7 NAG G 762 111.354 146.036 283.784 1.00 70.55 ATOM 2299 O7 NAG G 762 112.398 146.161 283.144 1.00 67.21 ATOM 2300 C8 NAG G 762 110.187 145.309 283.187 1.00 79.91 ATOM 2301 C3 NAG G 762 112.831 146.474 286.791 1.00 92.58 ATOM 2302 O3 NAG G 762 113.700 145.531 286.202 1.00 87.59 ATOM 2303 C4 NAG G 762 113.633 147.310 287.783 1.00 97.48 ATOM 2304 O4 NAG G 762 113.868 146.536 288.938 1.00 98.59 ATOM 2305 C5 NAG G 762 112.915 148.599 288.173 1.00 101.11 ATOM 2306 C6 NAG G 762 113.843 149.499 288.981 1.00 103.36 ATOM 2307 O6 NAG G 762 113.244 149.802 290.220 1.00 106.88 ATOM 2308 O5 NAG G 762 112.496 149.301 287.021 1.00 99.01 ATOM 2309 C1 NAG G 776 91.236 159.349 260.321 1.00 77.40 ATOM 2310 C2 NAG G 776 91.417 160.002 258.957 1.00 86.35 ATOM 2311 N2 NAG G 776 92.082 161.281 259.115 1.00 85.18 ATOM 2312 C7 NAG G 776 93.385 161.414 258.884 1.00 92.23 ATOM 2313 O7 NAG G 776 94.092 162.217 259.491 1.00 96.62 ATOM 2314 C8 NAG G 776 93.980 160.527 257.830 1.00 91.17 ATOM 2315 C3 NAG G 776 90.093 160.183 258.226 1.00 81.43 ATOM 2316 O3 NAG G 776 90.363 160.570 256.897 1.00 80.13 ATOM 2317 C4 NAG G 776 89.281 158.893 258.212 1.00 82.57 ATOM 2318 O4 NAG G 776 87.948 159.184 257.852 1.00 84.39 ATOM 2319 C5 NAG G 776 89.271 158.187 259.565 1.00 83.99 ATOM 2320 C6 NAG G 776 89.899 156.800 259.460 1.00 85.80 ATOM 2321 O6 NAG G 776 88.938 155.882 258.990 1.00 83.39 ATOM 2322 O5 NAG G 776 89.897 158.968 260.569 1.00 83.25 ATOM 2323 C1 NAG G 789 95.991 162.163 287.700 1.00 93.24 ATOM 2324 C2 NAG G 789 95.358 163.176 288.659 1.00 96.28 ATOM 2325 N2 NAG G 789 96.136 163.438 289.865 1.00 96.50 ATOM 2326 C7 NAG G 789 96.528 162.524 290.753 1.00 98.21 ATOM 2327 O7 NAG G 789 97.688 162.115 290.807 1.00 96.36 ATOM 2328 C8 NAG G 789 95.501 162.015 291.726 1.00 96.64 ATOM 2329 C3 NAG G 789 93.931 162.750 288.977 1.00 98.49 ATOM 2330 O3 NAG G 789 93.321 163.667 289.856 1.00 107.33 ATOM 2331 C4 NAG G 789 93.155 162.687 287.671 1.00 98.80 ATOM 2332 O4 NAG G 789 91.852 162.209 287.922 1.00 97.15 ATOM 2333 C5 NAG G 789 93.876 161.774 286.680 1.00 98.73 ATOM 2334 C6 NAG G 789 93.143 161.748 285.340 1.00 101.03 ATOM 2335 O6 NAG G 789 93.793 162.579 284.403 1.00 100.98 ATOM 2336 O5 NAG G 789 95.227 162.177 286.505 1.00 97.31 ATOM 2337 C1 NAG G 795 105.020 145.335 295.118 1.00 99.00 ATOM 2338 C2 NAG G 795 103.890 145.405 296.140 1.00 107.09 ATOM 2339 N2 NAG G 795 102.601 145.347 295.464 1.00 105.80 ATOM 2340 C7 NAG G 795 101.743 144.335 295.619 1.00 100.23 ATOM 2341 O7 NAG G 795 102.088 143.190 295.912 1.00 94.60 ATOM 2342 C8 NAG G 795 100.290 144.652 295.413 1.00 94.48 ATOM 2343 C3 NAG G 795 103.991 146.677 296.984 1.00 106.49 ATOM 2344 O3 NAG G 795 103.188 146.536 298.136 1.00 105.39 ATOM 2345 C4 NAG G 795 105.424 146.997 297.413 1.00 105.07 ATOM 2346 O4 NAG G 795 105.491 148.349 297.808 1.00 101.46 ATOM 2347 C5 NAG G 795 106.441 146.746 296.302 1.00 104.45 ATOM 2348 C6 NAG G 795 107.871 146.890 296.816 1.00 106.23 ATOM 2349 O6 NAG G 795 108.657 147.576 295.866 1.00 101.74 ATOM 2350 O5 NAG G 795 106.259 145.448 295.783 1.00 100.85 ATOM 2351 C1 NAG G 839 86.157 149.894 291.693 1.00 102.00 ATOM 2352 C2 NAG G 839 84.786 150.184 291.074 1.00 111.97 ATOM 2353 N2 NAG G 839 84.643 151.601 290.764 1.00 111.43 ATOM 2354 C7 NAG G 839 85.032 152.586 291.576 1.00 113.62 ATOM 2355 O7 NAG G 839 86.156 153.089 291.532 1.00 112.92 ATOM 2356 C8 NAG G 839 84.023 153.089 292.567 1.00 114.56 ATOM 2357 C3 NAG G 839 83.618 149.730 291.950 1.00 116.42 ATOM 2358 O3 NAG G 839 82.450 149.640 291.164 1.00 122.05 ATOM 2359 C4 NAG G 839 83.878 148.382 292.611 1.00 119.33 ATOM 2360 O4 NAG G 839 82.899 148.160 293.603 1.00 120.67 ATOM 2361 C5 NAG G 839 85.273 148.352 293.226 1.00 117.62 ATOM 2362 C6 NAG G 839 85.564 147.016 293.902 1.00 118.46 ATOM 2363 O6 NAG G 839 86.956 146.867 294.083 1.00 116.86 ATOM 2364 O5 NAG G 839 86.219 148.579 292.205 1.00 109.31 ATOM 2365 C1 NAG G 856 75.002 162.625 277.570 1.00 123.26 ATOM 2366 C2 NAG G 856 74.713 163.226 276.201 1.00 130.23 ATOM 2367 N2 NAG G 856 74.168 162.239 275.284 1.00 133.62 ATOM 2368 C7 NAG G 856 72.879 162.236 274.944 1.00 135.69 ATOM 2369 O7 NAG G 856 72.296 163.233 274.520 1.00 136.07 ATOM 2370 C8 NAG G 856 72.143 160.937 275.099 1.00 134.98 ATOM 2371 C3 NAG G 856 76.005 163.838 275.672 1.00 129.25 ATOM 2372 O3 NAG G 856 75.771 164.476 274.435 1.00 132.54 ATOM 2373 C4 NAG G 856 76.568 164.843 276.678 1.00 126.21 ATOM 2374 O4 NAG G 856 77.921 165.092 276.364 1.00 120.65 ATOM 2375 C5 NAG G 856 76.480 164.378 278.138 1.00 126.74 ATOM 2376 C6 NAG G 856 76.633 165.569 279.081 1.00 125.92 ATOM 2377 O6 NAG G 856 77.241 165.157 280.285 1.00 123.39 ATOM 2378 O5 NAG G 856 75.261 163.716 278.430 1.00 125.20 ATOM 2379 C1 NAG G 886 93.603 133.329 281.057 1.00 48.19 ATOM 2380 C2 NAG G 886 92.385 133.549 281.948 1.00 52.05 ATOM 2381 N2 NAG G 886 92.648 133.027 283.277 1.00 62.22 ATOM 2382 C7 NAG G 886 93.003 133.805 284.297 1.00 64.71 ATOM 2383 O7 NAG G 886 93.170 135.022 284.190 1.00 65.46 ATOM 2384 C8 NAG G 886 93.194 133.120 285.621 1.00 65.07 ATOM 2385 C3 NAG G 886 91.152 132.877 281.365 1.00 51.95 ATOM 2386 O3 NAG G 886 90.016 133.271 282.097 1.00 59.61 ATOM 2387 C4 NAG G 886 90.993 133.250 279.896 1.00 51.67 ATOM 2388 O4 NAG G 886 89.902 132.552 279.346 1.00 55.36 ATOM 2389 C5 NAG G 886 92.267 132.904 279.138 1.00 41.12 ATOM 2390 C6 NAG G 886 92.129 133.222 277.654 1.00 53.43 ATOM 2391 O6 NAG G 886 93.399 133.359 277.049 1.00 57.16 ATOM 2392 O5 NAG G 886 93.341 133.638 279.697 1.00 57.06 ATOM 2393 C1 NAG G 892 85.036 138.886 284.138 1.00 91.57 ATOM 2394 C2 NAG G 892 85.709 137.909 285.099 1.00 90.02 ATOM 2395 N2 NAG G 892 86.728 137.088 284.461 1.00 81.07 ATOM 2396 C7 NAG G 892 87.954 136.956 284.981 1.00 78.87 ATOM 2397 O7 NAG G 892 88.770 136.124 284.581 1.00 75.29 ATOM 2398 C8 NAG G 892 88.333 137.877 286.104 1.00 78.04 ATOM 2399 C3 NAG G 892 84.612 137.076 285.746 1.00 93.89 ATOM 2400 O3 NAG G 892 85.156 136.102 286.610 1.00 91.33 ATOM 2401 C4 NAG G 892 83.714 138.031 286.522 1.00 96.93 ATOM 2402 O4 NAG G 892 82.637 137.317 287.087 1.00 102.65 ATOM 2403 C5 NAG G 892 83.189 139.148 285.619 1.00 96.13 ATOM 2404 C6 NAG G 892 82.482 140.211 286.452 1.00 96.22 ATOM 2405 O6 NAG G 892 81.635 140.979 285.626 1.00 90.90 ATOM 2406 O5 NAG G 892 84.238 139.770 284.900 1.00 96.94 ATOM 2407 C1 NAG G 897 75.055 148.517 280.098 1.00 113.12 ATOM 2408 C2 NAG G 897 73.696 147.826 279.977 1.00 118.11 ATOM 2409 N2 NAG G 897 72.847 148.208 281.093 1.00 120.19 ATOM 2410 C7 NAG G 897 71.752 148.953 280.943 1.00 123.68 ATOM 2411 O7 NAG G 897 70.682 148.670 281.478 1.00 123.49 ATOM 2412 C8 NAG G 897 71.862 150.186 280.091 1.00 127.00 ATOM 2413 C3 NAG G 897 73.826 146.301 279.918 1.00 116.05 ATOM 2414 O3 NAG G 897 72.613 145.741 279.459 1.00 111.12 ATOM 2415 C4 NAG G 897 74.972 145.841 279.016 1.00 112.87 ATOM 2416 O4 NAG G 897 75.277 144.494 279.301 1.00 106.04 ATOM 2417 C5 NAG G 897 76.218 146.698 279.221 1.00 113.28 ATOM 2418 C6 NAG G 897 77.329 146.355 278.239 1.00 111.30 ATOM 2419 O6 NAG G 897 77.908 147.560 277.788 1.00 104.36 ATOM 2420 O5 NAG G 897 75.887 148.058 279.057 1.00 116.98 ATOM 2421 C1 NAG G 948 107.795 153.333 290.652 1.00 107.40 ATOM 2422 C2 NAG G 948 109.306 153.486 290.779 1.00 116.19 ATOM 2423 N2 NAG G 948 109.990 152.515 289.944 1.00 116.99 ATOM 2424 C7 NAG G 948 110.795 152.902 288.957 1.00 116.65 ATOM 2425 O7 NAG G 948 110.402 153.113 287.811 1.00 111.83 ATOM 2426 C8 NAG G 948 112.244 153.079 289.308 1.00 120.57 ATOM 2427 C3 NAG G 948 109.714 153.344 292.242 1.00 117.13 ATOM 2428 O3 NAG G 948 111.092 153.600 292.395 1.00 118.65 ATOM 2429 C4 NAG G 948 108.909 154.316 293.099 1.00 115.82 ATOM 2430 O4 NAG G 948 109.174 154.078 294.465 1.00 111.42 ATOM 2431 C5 NAG G 948 107.413 154.171 292.818 1.00 113.40 ATOM 2432 C6 NAG G 948 106.600 155.199 293.600 1.00 110.35 ATOM 2433 O6 NAG G 948 106.233 156.263 292.750 1.00 107.59 ATOM 2434 O5 NAG G 948 107.163 154.326 291.434 1.00 111.55 ATOM 2435 C1 NAG G 963 73.872 154.396 265.668 1.00 115.57 ATOM 2436 C2 NAG G 963 73.069 155.614 266.123 1.00 127.44 ATOM 2437 N2 NAG G 963 71.857 155.206 266.819 1.00 127.17 ATOM 2438 C7 NAG G 963 71.773 155.189 268.151 1.00 126.27 ATOM 2439 O7 NAG G 963 72.098 156.139 268.865 1.00 124.05 ATOM 2440 C8 NAG G 963 71.247 153.928 268.770 1.00 124.60 ATOM 2441 C3 NAG G 963 72.749 156.513 264.932 1.00 129.70 ATOM 2442 O3 NAG G 963 72.352 157.789 265.385 1.00 130.48 ATOM 2443 C4 NAG G 963 73.977 156.639 264.034 1.00 129.94 ATOM 2444 O4 NAG G 963 73.695 157.480 262.936 1.00 132.28 ATOM 2445 C5 NAG G 963 74.420 155.267 263.528 1.00 125.59 ATOM 2446 C6 NAG G 963 75.936 155.116 263.601 1.00 122.39 ATOM 2447 O6 NAG G 963 76.468 155.165 262.296 1.00 118.53 ATOM 2448 O5 NAG G 963 73.788 154.235 264.264 1.00 121.01 ATOM 2449 N GLN H 1 81.553 139.114 260.771 1.00 77.57 ATOM 2450 CA GLN H 1 82.055 137.785 260.313 1.00 73.69 ATOM 2451 CB GLN H 1 81.042 137.110 259.379 1.00 75.92 ATOM 2452 CG GLN H 1 79.894 138.006 258.964 1.00 86.50 ATOM 2453 CD GLN H 1 80.362 139.333 258.409 1.00 99.20 ATOM 2454 OE1 GLN H 1 81.330 139.397 257.650 1.00 107.24 ATOM 2455 NE2 GLN H 1 79.676 140.406 258.788 1.00 102.05 ATOM 2456 C GLN H 1 83.436 137.860 259.659 1.00 70.67 ATOM 2457 O GLN H 1 83.732 138.765 258.867 1.00 64.50 ATOM 2458 N VAL H 2 84.278 136.897 260.012 1.00 65.27 ATOM 2459 CA VAL H 2 85.631 136.839 259.510 1.00 62.87 ATOM 2460 CB VAL H 2 86.460 135.853 260.331 1.00 61.98 ATOM 2461 CG1 VAL H 2 87.879 135.793 259.804 1.00 62.54 ATOM 2462 CG2 VAL H 2 86.448 136.267 261.802 1.00 67.18 ATOM 2463 C VAL H 2 85.638 136.427 258.039 1.00 65.72 ATOM 2464 O VAL H 2 85.014 135.435 257.656 1.00 67.10 ATOM 2465 N GLN H 3 86.334 137.199 257.212 1.00 65.25 ATOM 2466 CA GLN H 3 86.386 136.925 255.778 1.00 67.70 ATOM 2467 CB GLN H 3 85.296 137.700 255.040 1.00 66.30 ATOM 2468 CG GLN H 3 83.887 137.207 255.301 1.00 85.22 ATOM 2469 CD GLN H 3 82.856 137.945 254.473 1.00 96.86 ATOM 2470 OE1 GLN H 3 83.200 138.741 253.596 1.00 98.33 ATOM 2471 NE2 GLN H 3 81.583 137.685 254.747 1.00 98.90 ATOM 2472 C GLN H 3 87.729 137.303 255.195 1.00 67.03 ATOM 2473 O GLN H 3 88.307 138.326 255.562 1.00 69.86 ATOM 2474 N LEU H 4 88.216 136.467 254.283 1.00 65.59 ATOM 2475 CA LEU H 4 89.409 136.760 253.509 1.00 63.63 ATOM 2476 CB LEU H 4 90.459 135.656 253.689 1.00 66.51 ATOM 2477 CG LEU H 4 91.565 135.779 254.746 1.00 71.77 ATOM 2478 CD1 LEU H 4 91.208 136.725 255.868 1.00 66.67 ATOM 2479 CD2 LEU H 4 91.934 134.406 255.290 1.00 62.93 ATOM 2480 C LEU H 4 89.011 136.856 252.048 1.00 62.93 ATOM 2481 O LEU H 4 88.440 135.918 251.494 1.00 64.21 ATOM 2482 N VAL H 5 89.312 137.997 251.434 1.00 61.24 ATOM 2483 CA VAL H 5 88.972 138.267 250.040 1.00 60.97 ATOM 2484 CB VAL H 5 88.196 139.594 249.906 1.00 61.28 ATOM 2485 CG1 VAL H 5 87.881 139.891 248.444 1.00 54.65 ATOM 2486 CG2 VAL H 5 86.926 139.548 250.736 1.00 59.93 ATOM 2487 C VAL H 5 90.252 138.345 249.203 1.00 61.87 ATOM 2488 O VAL H 5 91.134 139.169 249.464 1.00 63.65 ATOM 2489 N GLN H 6 90.350 137.479 248.201 1.00 59.18 ATOM 2490 CA GLN H 6 91.575 137.349 247.417 1.00 59.83 ATOM 2491 CB GLN H 6 91.949 135.872 247.246 1.00 58.25 ATOM 2492 CG GLN H 6 92.140 135.138 248.558 1.00 58.15 ATOM 2493 CD GLN H 6 92.775 133.775 248.387 1.00 59.19 ATOM 2494 OE1 GLN H 6 92.487 132.856 249.138 1.00 65.54 ATOM 2495 NE2 GLN H 6 93.648 133.640 247.397 1.00 63.11 ATOM 2496 C GLN H 6 91.439 138.018 246.060 1.00 59.60 ATOM 2497 O GLN H 6 90.332 138.178 245.546 1.00 62.76 ATOM 2498 N SER H 7 92.570 138.407 245.480 1.00 62.43 ATOM 2499 CA SER H 7 92.565 139.059 244.171 1.00 62.86 ATOM 2500 CB SER H 7 93.924 139.716 243.881 1.00 60.50 ATOM 2501 OG SER H 7 94.995 138.898 244.316 1.00 63.38 ATOM 2502 C SER H 7 92.155 138.097 243.045 1.00 61.92 ATOM 2503 O SER H 7 92.102 136.883 243.236 1.00 61.42 ATOM 2504 N GLY H 8 91.861 138.651 241.875 1.00 62.06 ATOM 2505 CA GLY H 8 91.330 137.867 240.771 1.00 61.02 ATOM 2506 C GLY H 8 92.353 136.969 240.112 1.00 60.86 ATOM 2507 O GLY H 8 93.558 137.109 240.344 1.00 59.90 ATOM 2508 N ALA H 9 91.855 136.054 239.280 1.00 58.85 ATOM 2509 CA ALA H 9 92.673 135.091 238.540 1.00 56.63 ATOM 2510 CB ALA H 9 91.791 134.269 237.613 1.00 54.28 ATOM 2511 C ALA H 9 93.806 135.730 237.746 1.00 60.50 ATOM 2512 O ALA H 9 93.675 136.855 237.250 1.00 62.32 ATOM 2513 N GLU H 10 94.904 134.990 237.602 1.00 60.89 ATOM 2514 CA GLU H 10 96.113 135.497 236.957 1.00 61.88 ATOM 2515 CB GLU H 10 97.176 135.788 238.018 1.00 68.31 ATOM 2516 CG GLU H 10 96.836 136.924 238.972 1.00 74.96 ATOM 2517 CD GLU H 10 97.419 138.255 238.536 1.00 81.86 ATOM 2518 OE1 GLU H 10 97.870 138.367 237.375 1.00 91.08 ATOM 2519 OE2 GLU H 10 97.429 139.192 239.360 1.00 82.62 ATOM 2520 C GLU H 10 96.695 134.535 235.919 1.00 60.97 ATOM 2521 O GLU H 10 96.775 133.330 236.150 1.00 62.96 ATOM 2522 N VAL H 11 97.118 135.086 234.784 1.00 62.49 ATOM 2523 CA VAL H 11 97.753 134.315 233.717 1.00 63.16 ATOM 2524 CB VAL H 11 96.964 134.439 232.394 1.00 62.67 ATOM 2525 CG1 VAL H 11 97.667 133.691 231.283 1.00 63.96 ATOM 2526 CG2 VAL H 11 95.541 133.925 232.572 1.00 70.33 ATOM 2527 C VAL H 11 99.173 134.834 233.496 1.00 61.22 ATOM 2528 O VAL H 11 99.364 136.006 233.190 1.00 60.04 ATOM 2529 N LYS H 12 100.167 133.966 233.651 1.00 60.15 ATOM 2530 CA LYS H 12 101.562 134.396 233.590 1.00 60.35 ATOM 2531 CB LYS H 12 102.165 134.446 234.998 1.00 64.03 ATOM 2532 CG LYS H 12 102.256 135.847 235.590 1.00 72.50 ATOM 2533 CD LYS H 12 100.918 136.343 236.100 1.00 72.94 ATOM 2534 CE LYS H 12 100.810 137.850 235.952 1.00 77.99 ATOM 2535 NZ LYS H 12 102.011 138.551 236.471 1.00 78.14 ATOM 2536 C LYS H 12 102.434 133.528 232.688 1.00 60.27 ATOM 2537 O LYS H 12 102.179 132.336 232.523 1.00 61.26 ATOM 2538 N LYS H 13 103.461 134.144 232.107 1.00 58.96 ATOM 2539 CA LYS H 13 104.474 133.428 231.337 1.00 58.44 ATOM 2540 CB LYS H 13 105.219 134.391 230.409 1.00 56.53 ATOM 2541 CG LYS H 13 104.327 135.252 229.530 1.00 64.24 ATOM 2542 CD LYS H 13 103.634 134.432 228.455 1.00 69.55 ATOM 2543 CE LYS H 13 102.554 135.247 227.763 1.00 81.40 ATOM 2544 NZ LYS H 13 101.405 135.530 228.678 1.00 92.14 ATOM 2545 C LYS H 13 105.479 132.774 232.279 1.00 58.13 ATOM 2546 O LYS H 13 105.746 133.297 233.360 1.00 58.31 ATOM 2547 N PRO H 14 106.053 131.631 231.870 1.00 59.38 ATOM 2548 CA PRO H 14 107.116 131.024 232.669 1.00 58.88 ATOM 2549 CB PRO H 14 107.608 129.878 231.783 1.00 57.55 ATOM 2550 CG PRO H 14 106.452 129.551 230.913 1.00 60.44 ATOM 2551 CD PRO H 14 105.757 130.852 230.656 1.00 60.27 ATOM 2552 C PRO H 14 108.243 132.031 232.892 1.00 58.13 ATOM 2553 O PRO H 14 108.520 132.844 232.012 1.00 56.16 ATOM 2554 N GLY H 15 108.874 131.985 234.060 1.00 57.42 ATOM 2555 CA GLY H 15 109.960 132.907 234.376 1.00 59.85 ATOM 2556 C GLY H 15 109.487 134.219 234.981 1.00 61.23 ATOM 2557 O GLY H 15 110.271 134.945 235.596 1.00 62.15 ATOM 2558 N ALA H 16 108.204 134.525 234.808 1.00 59.69 ATOM 2559 CA ALA H 16 107.621 135.738 235.367 1.00 57.81 ATOM 2560 CB ALA H 16 106.358 136.122 234.610 1.00 55.26 ATOM 2561 C ALA H 16 107.317 135.547 236.845 1.00 60.05 ATOM 2562 O ALA H 16 107.627 134.503 237.420 1.00 58.09 ATOM 2563 N SER H 17 106.714 136.563 237.456 1.00 62.29 ATOM 2564 CA SER H 17 106.315 136.492 238.856 1.00 64.09 ATOM 2565 CB SER H 17 107.255 137.320 239.736 1.00 65.44 ATOM 2566 OG SER H 17 106.979 138.705 239.623 1.00 76.20 ATOM 2567 C SER H 17 104.879 136.971 239.028 1.00 64.01 ATOM 2568 O SER H 17 104.368 137.739 238.213 1.00 62.12 ATOM 2569 N VAL H 18 104.236 136.515 240.097 1.00 63.66 ATOM 2570 CA VAL H 18 102.853 136.878 240.374 1.00 66.71 ATOM 2571 CB VAL H 18 101.885 135.706 240.054 1.00 65.81 ATOM 2572 CG1 VAL H 18 102.230 134.478 240.882 1.00 63.32 ATOM 2573 CG2 VAL H 18 100.445 136.119 240.282 1.00 64.04 ATOM 2574 C VAL H 18 102.705 137.296 241.834 1.00 67.42 ATOM 2575 O VAL H 18 103.298 136.684 242.724 1.00 69.06 ATOM 2576 N LYS H 19 101.927 138.347 242.069 1.00 65.15 ATOM 2577 CA LYS H 19 101.642 138.809 243.422 1.00 63.12 ATOM 2578 CB LYS H 19 102.104 140.259 243.606 1.00 65.03 ATOM 2579 CG LYS H 19 102.170 140.708 245.059 1.00 64.29 ATOM 2580 CD LYS H 19 102.854 142.062 245.199 1.00 74.56 ATOM 2581 CE LYS H 19 102.847 142.522 246.651 1.00 78.45 ATOM 2582 NZ LYS H 19 103.522 143.830 246.859 1.00 79.35 ATOM 2583 C LYS H 19 100.150 138.675 243.719 1.00 63.61 ATOM 2584 O LYS H 19 99.313 139.330 243.095 1.00 65.63 ATOM 2585 N VAL H 20 99.827 137.807 244.669 1.00 62.77 ATOM 2586 CA VAL H 20 98.453 137.553 245.060 1.00 63.32 ATOM 2587 CB VAL H 20 98.198 136.034 245.225 1.00 63.78 ATOM 2588 CG1 VAL H 20 96.781 135.778 245.716 1.00 70.34 ATOM 2589 CG2 VAL H 20 98.441 135.302 243.915 1.00 65.60 ATOM 2590 C VAL H 20 98.159 138.262 246.381 1.00 64.84 ATOM 2591 O VAL H 20 98.933 138.153 247.335 1.00 61.23 ATOM 2592 N SER H 21 97.039 138.978 246.444 1.00 64.15 ATOM 2593 CA SER H 21 96.686 139.703 247.659 1.00 63.20 ATOM 2594 CB SER H 21 96.320 141.151 247.342 1.00 61.38 ATOM 2595 OG SER H 21 95.080 141.213 246.673 1.00 62.50 ATOM 2596 C SER H 21 95.548 139.030 248.417 1.00 67.27 ATOM 2597 O SER H 21 94.745 138.295 247.839 1.00 65.70 ATOM 2598 N CYS H 22 95.484 139.307 249.716 1.00 69.59 ATOM 2599 CA CYS H 22 94.517 138.679 250.602 1.00 64.17 ATOM 2600 CB CYS H 22 95.152 137.472 251.288 1.00 65.60 ATOM 2601 SG CYS H 22 94.104 136.660 252.504 1.00 74.11 ATOM 2602 C CYS H 22 94.031 139.678 251.641 1.00 63.26 ATOM 2603 O CYS H 22 94.743 139.989 252.601 1.00 61.81 ATOM 2604 N GLN H 23 92.813 140.176 251.456 1.00 60.15 ATOM 2605 CA GLN H 23 92.312 141.231 252.323 1.00 60.43 ATOM 2606 CB GLN H 23 91.681 142.357 251.511 1.00 57.22 ATOM 2607 CG GLN H 23 91.369 143.576 252.349 1.00 50.54 ATOM 2608 CD GLN H 23 90.762 144.696 251.537 1.00 64.00 ATOM 2609 OE1 GLN H 23 89.883 144.471 250.705 1.00 65.21 ATOM 2610 NE2 GLN H 23 91.225 145.917 251.779 1.00 57.56 ATOM 2611 C GLN H 23 91.337 140.731 253.376 1.00 62.98 ATOM 2612 O GLN H 23 90.379 140.019 253.075 1.00 65.39 ATOM 2613 N ALA H 24 91.588 141.127 254.617 1.00 64.41 ATOM 2614 CA ALA H 24 90.804 140.669 255.757 1.00 60.06 ATOM 2615 CB ALA H 24 91.729 140.353 256.911 1.00 58.48 ATOM 2616 C ALA H 24 89.762 141.698 256.191 1.00 59.82 ATOM 2617 O ALA H 24 89.958 142.906 256.032 1.00 61.22 ATOM 2618 N SER H 25 88.651 141.202 256.727 1.00 57.06 ATOM 2619 CA SER H 25 87.653 142.026 257.397 1.00 59.64 ATOM 2620 CB SER H 25 86.612 142.545 256.399 1.00 63.06 ATOM 2621 OG SER H 25 86.029 141.478 255.680 1.00 66.69 ATOM 2622 C SER H 25 86.981 141.199 258.496 1.00 60.14 ATOM 2623 O SER H 25 87.073 139.967 258.494 1.00 58.56 ATOM 2624 N GLY H 26 86.331 141.877 259.439 1.00 54.71 ATOM 2625 CA GLY H 26 85.616 141.199 260.518 1.00 59.44 ATOM 2626 C GLY H 26 86.467 140.835 261.727 1.00 60.02 ATOM 2627 O GLY H 26 85.975 140.231 262.676 1.00 59.90 ATOM 2628 N TYR H 27 87.744 141.199 261.695 1.00 56.89 ATOM 2629 CA TYR H 27 88.651 140.935 262.810 1.00 58.48 ATOM 2630 CB TYR H 27 89.059 139.455 262.848 1.00 58.60 ATOM 2631 CG TYR H 27 90.118 139.080 261.833 1.00 58.02 ATOM 2632 CD1 TYR H 27 91.471 139.096 262.167 1.00 57.52 ATOM 2633 CE1 TYR H 27 92.444 138.758 261.229 1.00 61.97 ATOM 2634 CZ TYR H 27 92.062 138.404 259.943 1.00 52.98 ATOM 2635 OH TYR H 27 93.004 138.063 259.006 1.00 62.87 ATOM 2636 CE2 TYR H 27 90.735 138.377 259.593 1.00 54.13 ATOM 2637 CD2 TYR H 27 89.768 138.715 260.539 1.00 61.07 ATOM 2638 C TYR H 27 89.885 141.828 262.682 1.00 60.54 ATOM 2639 O TYR H 27 90.094 142.473 261.645 1.00 57.65 ATOM 2640 N ARG H 28 90.706 141.858 263.728 1.00 64.12 ATOM 2641 CA ARG H 28 91.917 142.678 263.714 1.00 65.05 ATOM 2642 CB ARG H 28 92.387 142.990 265.133 1.00 65.95 ATOM 2643 CG ARG H 28 93.414 144.093 265.179 1.00 62.02 ATOM 2644 CD ARG H 28 93.251 144.953 266.407 1.00 67.50 ATOM 2645 NE ARG H 28 93.678 146.320 266.134 1.00 82.98 ATOM 2646 CZ ARG H 28 92.847 147.333 265.910 1.00 76.31 ATOM 2647 NH1 ARG H 28 93.333 148.538 265.667 1.00 96.92 ATOM 2648 NH2 ARG H 28 91.533 147.148 265.949 1.00 79.86 ATOM 2649 C ARG H 28 93.030 142.012 262.910 1.00 63.85 ATOM 2650 O ARG H 28 93.695 141.089 263.384 1.00 62.58 ATOM 2651 N PHE H 29 93.223 142.500 261.691 1.00 61.14 ATOM 2652 CA PHE H 29 94.121 141.872 260.723 1.00 60.56 ATOM 2653 CB PHE H 29 94.212 142.731 259.458 1.00 58.99 ATOM 2654 CG PHE H 29 95.312 142.320 258.523 1.00 63.76 ATOM 2655 CD1 PHE H 29 95.213 141.152 257.783 1.00 62.25 ATOM 2656 CE1 PHE H 29 96.226 140.778 256.922 1.00 57.64 ATOM 2657 CZ PHE H 29 97.350 141.565 256.796 1.00 57.43 ATOM 2658 CE2 PHE H 29 97.461 142.724 257.526 1.00 64.49 ATOM 2659 CD2 PHE H 29 96.443 143.100 258.382 1.00 58.40 ATOM 2660 C PHE H 29 95.523 141.583 261.256 1.00 60.50 ATOM 2661 O PHE H 29 96.068 140.503 261.035 1.00 62.26 ATOM 2662 N SER H 30 96.104 142.557 261.946 1.00 58.60 ATOM 2663 CA SER H 30 97.486 142.463 262.393 1.00 59.81 ATOM 2664 CB SER H 30 97.950 143.822 262.911 1.00 58.87 ATOM 2665 OG SER H 30 97.325 144.106 264.149 1.00 57.85 ATOM 2666 C SER H 30 97.692 141.424 263.492 1.00 60.65 ATOM 2667 O SER H 30 98.823 141.086 263.827 1.00 63.96 ATOM 2668 N ASN H 31 96.603 140.921 264.058 1.00 61.50 ATOM 2669 CA ASN H 31 96.699 140.068 265.234 1.00 61.48 ATOM 2670 CB ASN H 31 95.605 140.426 266.240 1.00 58.24 ATOM 2671 CG ASN H 31 95.924 141.689 267.017 1.00 63.35 ATOM 2672 OD1 ASN H 31 96.602 142.592 266.519 1.00 67.21 ATOM 2673 ND2 ASN H 31 95.446 141.752 268.251 1.00 58.15 ATOM 2674 C ASN H 31 96.681 138.573 264.960 1.00 64.09 ATOM 2675 O ASN H 31 96.760 137.773 265.889 1.00 63.43 ATOM 2676 N PHE H 32 96.578 138.186 263.695 1.00 64.78 ATOM 2677 CA PHE H 32 96.582 136.764 263.356 1.00 64.08 ATOM 2678 CB PHE H 32 95.177 136.289 262.989 1.00 62.66 ATOM 2679 CG PHE H 32 94.182 136.381 264.110 1.00 66.84 ATOM 2680 CD1 PHE H 32 93.827 135.250 264.829 1.00 55.37 ATOM 2681 CE1 PHE H 32 92.904 135.325 265.852 1.00 63.20 ATOM 2682 CZ PHE H 32 92.320 136.535 266.163 1.00 58.77 ATOM 2683 CE2 PHE H 32 92.662 137.675 265.451 1.00 59.81 ATOM 2684 CD2 PHE H 32 93.582 137.593 264.427 1.00 60.33 ATOM 2685 C PHE H 32 97.515 136.463 262.195 1.00 61.98 ATOM 2686 O PHE H 32 97.470 137.120 261.156 1.00 67.79 ATOM 2687 N VAL H 33 98.346 135.447 262.372 1.00 62.19 ATOM 2688 CA VAL H 33 99.188 134.938 261.301 1.00 61.32 ATOM 2689 CB VAL H 33 100.026 133.752 261.809 1.00 61.64 ATOM 2690 CG1 VAL H 33 100.505 132.869 260.666 1.00 52.86 ATOM 2691 CG2 VAL H 33 101.200 134.260 262.650 1.00 64.62 ATOM 2692 C VAL H 33 98.335 134.535 260.090 1.00 62.41 ATOM 2693 O VAL H 33 97.179 134.144 260.239 1.00 60.18 ATOM 2694 N ILE H 34 98.907 134.666 258.895 1.00 61.97 ATOM 2695 CA ILE H 34 98.250 134.255 257.648 1.00 60.30 ATOM 2696 CB ILE H 34 98.003 135.477 256.718 1.00 64.62 ATOM 2697 CG1 ILE H 34 96.804 136.290 257.223 1.00 60.91 ATOM 2698 CD1 ILE H 34 96.374 137.376 256.291 1.00 82.34 ATOM 2699 CG2 ILE H 34 97.778 135.041 255.268 1.00 61.60 ATOM 2700 C ILE H 34 99.080 133.191 256.922 1.00 62.07 ATOM 2701 O ILE H 34 100.279 133.367 256.708 1.00 59.28 ATOM 2702 N HIS H 35 98.445 132.074 256.579 1.00 60.59 ATOM 2703 CA HIS H 35 99.102 131.009 255.825 1.00 54.75 ATOM 2704 CB HIS H 35 98.562 129.635 256.216 1.00 57.34 ATOM 2705 CG HIS H 35 99.166 129.069 257.460 1.00 59.80 ATOM 2706 ND1 HIS H 35 98.422 128.786 258.585 1.00 62.72 ATOM 2707 CE1 HIS H 35 99.213 128.283 259.516 1.00 68.75 ATOM 2708 NE2 HIS H 35 100.443 128.229 259.035 1.00 62.03 ATOM 2709 CD2 HIS H 35 100.439 128.712 257.749 1.00 55.41 ATOM 2710 C HIS H 35 98.840 131.176 254.346 1.00 61.31 ATOM 2711 O HIS H 35 97.797 131.704 253.941 1.00 60.40 ATOM 2712 N TRP H 36 99.780 130.693 253.540 1.00 58.21 ATOM 2713 CA TRP H 36 99.570 130.565 252.106 1.00 57.82 ATOM 2714 CB TRP H 36 100.562 131.437 251.346 1.00 57.56 ATOM 2715 CG TRP H 36 100.290 132.899 251.499 1.00 59.54 ATOM 2716 CD1 TRP H 36 100.847 133.746 252.410 1.00 60.40 ATOM 2717 NE1 TRP H 36 100.349 135.013 252.241 1.00 60.82 ATOM 2718 CE2 TRP H 36 99.446 135.001 251.212 1.00 64.91 ATOM 2719 CD2 TRP H 36 99.379 133.682 250.724 1.00 57.72 ATOM 2720 CE3 TRP H 36 98.527 133.400 249.651 1.00 60.88 ATOM 2721 CZ3 TRP H 36 97.782 134.432 249.108 1.00 55.55 ATOM 2722 CH2 TRP H 36 97.865 135.733 249.619 1.00 60.08 ATOM 2723 CZ2 TRP H 36 98.689 136.039 250.667 1.00 64.57 ATOM 2724 C TRP H 36 99.725 129.106 251.697 1.00 60.51 ATOM 2725 O TRP H 36 100.707 128.446 252.071 1.00 58.39 ATOM 2726 N VAL H 37 98.752 128.618 250.929 1.00 59.47 ATOM 2727 CA VAL H 37 98.656 127.213 250.550 1.00 60.42 ATOM 2728 CB VAL H 37 97.643 126.472 251.469 1.00 62.73 ATOM 2729 CG1 VAL H 37 97.430 125.046 251.020 1.00 63.14 ATOM 2730 CG2 VAL H 37 98.107 126.499 252.921 1.00 65.08 ATOM 2731 C VAL H 37 98.179 127.140 249.101 1.00 63.23 ATOM 2732 O VAL H 37 97.344 127.941 248.686 1.00 65.18 ATOM 2733 N ARG H 38 98.711 126.201 248.324 1.00 62.67 ATOM 2734 CA ARG H 38 98.286 126.032 246.928 1.00 64.59 ATOM 2735 CB ARG H 38 99.441 126.291 245.946 1.00 62.28 ATOM 2736 CG ARG H 38 100.726 125.584 246.327 1.00 72.18 ATOM 2737 CD ARG H 38 101.405 124.866 245.164 1.00 76.85 ATOM 2738 NE ARG H 38 102.123 125.767 244.276 1.00 70.54 ATOM 2739 CZ ARG H 38 103.182 125.425 243.546 1.00 65.99 ATOM 2740 NH1 ARG H 38 103.682 124.198 243.605 1.00 59.97 ATOM 2741 NH2 ARG H 38 103.759 126.328 242.768 1.00 68.11 ATOM 2742 C ARG H 38 97.767 124.628 246.683 1.00 62.56 ATOM 2743 O ARG H 38 98.078 123.698 247.427 1.00 60.61 ATOM 2744 N GLN H 39 96.981 124.480 245.625 1.00 62.18 ATOM 2745 CA GLN H 39 96.656 123.161 245.118 1.00 60.06 ATOM 2746 CB GLN H 39 95.331 122.643 245.675 1.00 57.64 ATOM 2747 CG GLN H 39 95.049 121.229 245.207 1.00 56.76 ATOM 2748 CD GLN H 39 93.816 120.635 245.833 1.00 63.67 ATOM 2749 OE1 GLN H 39 92.774 121.285 245.926 1.00 60.73 ATOM 2750 NE2 GLN H 39 93.922 119.381 246.263 1.00 52.63 ATOM 2751 C GLN H 39 96.617 123.168 243.598 1.00 61.13 ATOM 2752 O GLN H 39 95.746 123.794 242.999 1.00 65.08 ATOM 2753 N ALA H 40 97.574 122.469 242.991 1.00 59.12 ATOM 2754 CA ALA H 40 97.644 122.291 241.544 1.00 62.36 ATOM 2755 CB ALA H 40 99.102 122.006 241.115 1.00 54.46 ATOM 2756 C ALA H 40 96.724 121.148 241.097 1.00 62.14 ATOM 2757 O ALA H 40 96.436 120.241 241.879 1.00 63.91 ATOM 2758 N PRO H 41 96.264 121.189 239.832 1.00 64.22 ATOM 2759 CA PRO H 41 95.390 120.152 239.290 1.00 62.75 ATOM 2760 CB PRO H 41 95.501 120.364 237.781 1.00 64.12 ATOM 2761 CG PRO H 41 95.757 121.824 237.630 1.00 67.29 ATOM 2762 CD PRO H 41 96.554 122.244 238.842 1.00 64.92 ATOM 2763 C PRO H 41 95.872 118.750 239.642 1.00 62.82 ATOM 2764 O PRO H 41 96.990 118.379 239.299 1.00 63.14 ATOM 2765 N GLY H 42 95.029 117.986 240.326 1.00 61.94 ATOM 2766 CA GLY H 42 95.336 116.597 240.649 1.00 66.26 ATOM 2767 C GLY H 42 96.312 116.398 241.798 1.00 67.17 ATOM 2768 O GLY H 42 96.611 115.267 242.166 1.00 68.88 ATOM 2769 N GLN H 43 96.806 117.494 242.368 1.00 67.58 ATOM 2770 CA GLN H 43 97.794 117.427 243.440 1.00 63.43 ATOM 2771 CB GLN H 43 98.904 118.451 243.194 1.00 66.93 ATOM 2772 CG GLN H 43 99.630 118.263 241.875 1.00 64.21 ATOM 2773 CD GLN H 43 100.174 116.861 241.727 1.00 76.26 ATOM 2774 OE1 GLN H 43 100.930 116.383 242.574 1.00 79.69 ATOM 2775 NE2 GLN H 43 99.785 116.188 240.653 1.00 78.81 ATOM 2776 C GLN H 43 97.158 117.678 244.802 1.00 64.91 ATOM 2777 O GLN H 43 96.012 118.122 244.887 1.00 60.77 ATOM 2778 N ARG H 44 97.905 117.392 245.865 1.00 63.75 ATOM 2779 CA ARG H 44 97.464 117.710 247.218 1.00 62.83 ATOM 2780 CB ARG H 44 98.253 116.909 248.249 1.00 60.09 ATOM 2781 CG ARG H 44 98.248 115.427 248.015 1.00 61.78 ATOM 2782 CD ARG H 44 98.942 114.706 249.144 1.00 61.88 ATOM 2783 NE ARG H 44 98.965 113.269 248.903 1.00 62.47 ATOM 2784 CZ ARG H 44 99.190 112.362 249.841 1.00 54.02 ATOM 2785 NH1 ARG H 44 99.410 112.738 251.091 1.00 61.55 ATOM 2786 NH2 ARG H 44 99.187 111.079 249.529 1.00 53.53 ATOM 2787 C ARG H 44 97.674 119.189 247.495 1.00 63.95 ATOM 2788 O ARG H 44 98.421 119.863 246.784 1.00 65.60 ATOM 2789 N PHE H 45 97.020 119.690 248.535 1.00 62.01 ATOM 2790 CA PHE H 45 97.316 121.022 249.031 1.00 62.00 ATOM 2791 CB PHE H 45 96.438 121.346 250.226 1.00 64.35 ATOM 2792 CG PHE H 45 95.029 121.712 249.877 1.00 60.21 ATOM 2793 CD1 PHE H 45 94.010 120.783 249.997 1.00 62.83 ATOM 2794 CE1 PHE H 45 92.704 121.131 249.705 1.00 71.47 ATOM 2795 CZ PHE H 45 92.405 122.422 249.302 1.00 62.16 ATOM 2796 CE2 PHE H 45 93.412 123.356 249.188 1.00 59.05 ATOM 2797 CD2 PHE H 45 94.715 123.000 249.483 1.00 56.33 ATOM 2798 C PHE H 45 98.775 121.073 249.473 1.00 61.66 ATOM 2799 O PHE H 45 99.278 120.124 250.072 1.00 59.18 ATOM 2800 N GLU H 46 99.446 122.183 249.180 1.00 60.33 ATOM 2801 CA GLU H 46 100.846 122.364 249.559 1.00 60.99 ATOM 2802 CB GLU H 46 101.722 122.512 248.321 1.00 58.50 ATOM 2803 CG GLU H 46 102.215 121.237 247.723 1.00 70.38 ATOM 2804 CD GLU H 46 103.160 121.499 246.573 1.00 68.29 ATOM 2805 OE1 GLU H 46 102.753 122.207 245.627 1.00 67.17 ATOM 2806 OE2 GLU H 46 104.302 120.995 246.616 1.00 68.59 ATOM 2807 C GLU H 46 100.989 123.637 250.359 1.00 59.11 ATOM 2808 O GLU H 46 100.619 124.711 249.884 1.00 59.19 ATOM 2809 N TRP H 47 101.544 123.528 251.557 1.00 55.88 ATOM 2810 CA TRP H 47 101.796 124.706 252.372 1.00 58.72 ATOM 2811 CB TRP H 47 101.950 124.310 253.839 1.00 54.50 ATOM 2812 CG TRP H 47 102.376 125.430 254.739 1.00 58.14 ATOM 2813 CD1 TRP H 47 101.594 126.447 255.216 1.00 54.22 ATOM 2814 NE1 TRP H 47 102.341 127.277 256.022 1.00 58.67 ATOM 2815 CE2 TRP H 47 103.625 126.799 256.088 1.00 59.85 ATOM 2816 CD2 TRP H 47 103.686 125.634 255.292 1.00 52.24 ATOM 2817 CE3 TRP H 47 104.901 124.943 255.193 1.00 62.70 ATOM 2818 CZ3 TRP H 47 106.005 125.432 255.879 1.00 52.24 ATOM 2819 CH2 TRP H 47 105.913 126.598 256.663 1.00 56.46 ATOM 2820 CZ2 TRP H 47 104.738 127.292 256.779 1.00 56.30 ATOM 2821 C TRP H 47 103.041 125.427 251.867 1.00 56.85 ATOM 2822 O TRP H 47 104.083 124.809 251.669 1.00 60.70 ATOM 2823 N MET H 48 102.928 126.733 251.657 1.00 59.09 ATOM 2824 CA MET H 48 104.039 127.514 251.130 1.00 57.57 ATOM 2825 CB MET H 48 103.549 128.458 250.041 1.00 56.29 ATOM 2826 CG MET H 48 102.845 127.752 248.895 1.00 60.05 ATOM 2827 SD MET H 48 102.176 128.924 247.707 1.00 71.02 ATOM 2828 CE MET H 48 103.678 129.724 247.147 1.00 63.77 ATOM 2829 C MET H 48 104.757 128.296 252.221 1.00 56.94 ATOM 2830 O MET H 48 105.986 128.412 252.209 1.00 61.26 ATOM 2831 N GLY H 49 103.992 128.836 253.162 1.00 55.27 ATOM 2832 CA GLY H 49 104.578 129.529 254.301 1.00 55.60 ATOM 2833 C GLY H 49 103.571 130.369 255.051 1.00 58.84 ATOM 2834 O GLY H 49 102.388 130.375 254.715 1.00 61.91 ATOM 2835 N TRP H 50 104.032 131.076 256.079 1.00 61.36 ATOM 2836 CA TRP H 50 103.179 132.058 256.748 1.00 63.90 ATOM 2837 CB TRP H 50 102.497 131.491 258.005 1.00 60.08 ATOM 2838 CG TRP H 50 103.374 130.868 259.063 1.00 63.70 ATOM 2839 CD1 TRP H 50 103.506 129.535 259.327 1.00 66.27 ATOM 2840 NE1 TRP H 50 104.365 129.342 260.380 1.00 66.66 ATOM 2841 CE2 TRP H 50 104.803 130.561 260.829 1.00 63.59 ATOM 2842 CD2 TRP H 50 104.196 131.548 260.030 1.00 58.51 ATOM 2843 CE3 TRP H 50 104.483 132.892 260.289 1.00 59.09 ATOM 2844 CZ3 TRP H 50 105.353 133.201 261.319 1.00 65.41 ATOM 2845 CH2 TRP H 50 105.949 132.196 262.092 1.00 60.56 ATOM 2846 CZ2 TRP H 50 105.687 130.874 261.866 1.00 62.81 ATOM 2847 C TRP H 50 103.878 133.383 257.044 1.00 66.54 ATOM 2848 O TRP H 50 105.111 133.459 257.069 1.00 66.33 ATOM 2849 N ILE H 51 103.076 134.430 257.226 1.00 63.60 ATOM 2850 CA ILE H 51 103.579 135.715 257.678 1.00 58.74 ATOM 2851 CB ILE H 51 103.513 136.786 256.574 1.00 60.42 ATOM 2852 CG1 ILE H 51 103.973 138.145 257.127 1.00 59.51 ATOM 2853 CD1 ILE H 51 104.378 139.161 256.078 1.00 54.61 ATOM 2854 CG2 ILE H 51 102.104 136.869 256.006 1.00 61.33 ATOM 2855 C ILE H 51 102.771 136.183 258.885 1.00 60.08 ATOM 2856 O ILE H 51 101.568 135.936 258.977 1.00 59.67 ATOM 2857 N ASN H 52 103.450 136.846 259.813 1.00 58.82 ATOM 2858 CA ASN H 52 102.814 137.428 260.980 1.00 62.41 ATOM 2859 CB ASN H 52 103.573 137.027 262.250 1.00 62.08 ATOM 2860 CG ASN H 52 102.887 137.502 263.515 1.00 68.94 ATOM 2861 OD1 ASN H 52 102.185 138.514 263.514 1.00 69.71 ATOM 2862 ND2 ASN H 52 103.091 136.773 264.608 1.00 68.88 ATOM 2863 C ASN H 52 102.774 138.945 260.839 1.00 60.78 ATOM 2864 O ASN H 52 103.806 139.610 260.950 1.00 61.25 ATOM 2865 N PRO H 53 101.577 139.497 260.587 1.00 63.94 ATOM 2866 CA PRO H 53 101.406 140.934 260.355 1.00 60.75 ATOM 2867 CB PRO H 53 99.910 141.067 260.033 1.00 56.99 ATOM 2868 CG PRO H 53 99.457 139.692 259.686 1.00 58.64 ATOM 2869 CD PRO H 53 100.298 138.770 260.503 1.00 61.74 ATOM 2870 C PRO H 53 101.769 141.788 261.576 1.00 61.16 ATOM 2871 O PRO H 53 102.080 142.968 261.434 1.00 63.39 ATOM 2872 N TYR H 54 101.743 141.185 262.758 1.00 60.22 ATOM 2873 CA TYR H 54 102.048 141.887 263.999 1.00 62.03 ATOM 2874 CB TYR H 54 101.585 141.039 265.189 1.00 61.52 ATOM 2875 CG TYR H 54 101.845 141.643 266.548 1.00 55.82 ATOM 2876 CD1 TYR H 54 101.068 142.693 267.023 1.00 61.88 ATOM 2877 CE1 TYR H 54 101.296 143.246 268.278 1.00 61.26 ATOM 2878 CZ TYR H 54 102.305 142.738 269.074 1.00 66.14 ATOM 2879 OH TYR H 54 102.533 143.284 270.322 1.00 66.14 ATOM 2880 CE2 TYR H 54 103.087 141.688 268.627 1.00 58.94 ATOM 2881 CD2 TYR H 54 102.851 141.143 267.373 1.00 56.63 ATOM 2882 C TYR H 54 103.531 142.242 264.143 1.00 62.11 ATOM 2883 O TYR H 54 103.870 143.317 264.645 1.00 65.97 ATOM 2884 N ASN H 55 104.414 141.346 263.707 1.00 59.59 ATOM 2885 CA ASN H 55 105.853 141.556 263.888 1.00 60.55 ATOM 2886 CB ASN H 55 106.387 140.657 265.005 1.00 62.02 ATOM 2887 CG ASN H 55 106.096 139.194 264.757 1.00 62.42 ATOM 2888 OD1 ASN H 55 105.940 138.770 263.613 1.00 65.31 ATOM 2889 ND2 ASN H 55 106.010 138.415 265.827 1.00 66.83 ATOM 2890 C ASN H 55 106.687 141.357 262.626 1.00 61.59 ATOM 2891 O ASN H 55 107.898 141.551 262.646 1.00 64.16 ATOM 2892 N GLY H 56 106.043 140.965 261.534 1.00 63.18 ATOM 2893 CA GLY H 56 106.742 140.794 260.267 1.00 59.07 ATOM 2894 C GLY H 56 107.478 139.473 260.173 1.00 60.43 ATOM 2895 O GLY H 56 108.163 139.211 259.187 1.00 65.02 ATOM 2896 N ASN H 57 107.351 138.638 261.199 1.00 60.24 ATOM 2897 CA ASN H 57 107.968 137.317 261.165 1.00 62.51 ATOM 2898 CB ASN H 57 107.933 136.648 262.541 1.00 60.01 ATOM 2899 CG ASN H 57 109.061 137.108 263.441 1.00 67.11 ATOM 2900 OD1 ASN H 57 109.810 138.030 263.105 1.00 75.85 ATOM 2901 ND2 ASN H 57 109.192 136.464 264.594 1.00 70.15 ATOM 2902 C ASN H 57 107.309 136.427 260.119 1.00 64.66 ATOM 2903 O ASN H 57 106.105 136.527 259.868 1.00 65.05 ATOM 2904 N LYS H 58 108.115 135.566 259.507 1.00 62.96 ATOM 2905 CA LYS H 58 107.665 134.714 258.423 1.00 64.34 ATOM 2906 CB LYS H 58 108.099 135.299 257.075 1.00 68.37 ATOM 2907 CG LYS H 58 107.790 136.779 256.902 1.00 72.73 ATOM 2908 CD LYS H 58 108.784 137.457 255.970 1.00 73.08 ATOM 2909 CE LYS H 58 108.513 138.951 255.885 1.00 75.42 ATOM 2910 NZ LYS H 58 109.053 139.559 254.636 1.00 76.64 ATOM 2911 C LYS H 58 108.250 133.314 258.574 1.00 64.93 ATOM 2912 O LYS H 58 109.218 133.104 259.303 1.00 65.34 ATOM 2913 N GLU H 59 107.652 132.360 257.874 1.00 64.32 ATOM 2914 CA GLU H 59 108.154 131.000 257.827 1.00 62.98 ATOM 2915 CB GLU H 59 107.461 130.137 258.879 1.00 64.68 ATOM 2916 CG GLU H 59 108.073 128.759 259.077 1.00 72.23 ATOM 2917 CD GLU H 59 107.811 128.216 260.467 1.00 86.88 ATOM 2918 OE1 GLU H 59 108.411 128.740 261.432 1.00 99.00 ATOM 2919 OE2 GLU H 59 107.010 127.269 260.600 1.00 83.81 ATOM 2920 C GLU H 59 107.891 130.468 256.429 1.00 60.47 ATOM 2921 O GLU H 59 106.866 130.777 255.822 1.00 61.99 ATOM 2922 N PHE H 60 108.824 129.684 255.908 1.00 58.47 ATOM 2923 CA PHE H 60 108.737 129.234 254.530 1.00 61.32 ATOM 2924 CB PHE H 60 109.863 129.855 253.694 1.00 63.37 ATOM 2925 CG PHE H 60 109.899 131.359 253.738 1.00 65.15 ATOM 2926 CD1 PHE H 60 110.606 132.023 254.732 1.00 59.94 ATOM 2927 CE1 PHE H 60 110.642 133.408 254.774 1.00 65.14 ATOM 2928 CZ PHE H 60 109.972 134.147 253.815 1.00 64.05 ATOM 2929 CE2 PHE H 60 109.265 133.495 252.815 1.00 67.55 ATOM 2930 CD2 PHE H 60 109.232 132.109 252.781 1.00 67.73 ATOM 2931 C PHE H 60 108.824 127.721 254.432 1.00 60.97 ATOM 2932 O PHE H 60 109.541 127.081 255.198 1.00 60.68 ATOM 2933 N SER H 61 108.084 127.158 253.483 1.00 60.89 ATOM 2934 CA SER H 61 108.288 125.783 253.063 1.00 60.07 ATOM 2935 CB SER H 61 107.168 125.369 252.105 1.00 59.16 ATOM 2936 OG SER H 61 107.502 124.202 251.377 1.00 62.12 ATOM 2937 C SER H 61 109.641 125.717 252.359 1.00 59.42 ATOM 2938 O SER H 61 109.971 126.605 251.579 1.00 62.58 ATOM 2939 N ALA H 62 110.430 124.683 252.637 1.00 61.77 ATOM 2940 CA ALA H 62 111.737 124.539 251.989 1.00 60.43 ATOM 2941 CB ALA H 62 112.474 123.319 252.517 1.00 58.61 ATOM 2942 C ALA H 62 111.608 124.468 250.469 1.00 60.49 ATOM 2943 O ALA H 62 112.527 124.837 249.745 1.00 61.30 ATOM 2944 N LYS H 63 110.458 124.003 249.992 1.00 63.41 ATOM 2945 CA LYS H 63 110.219 123.864 248.560 1.00 66.63 ATOM 2946 CB LYS H 63 108.950 123.039 248.315 1.00 68.40 ATOM 2947 CG LYS H 63 108.635 122.764 246.844 1.00 69.90 ATOM 2948 CD LYS H 63 107.233 122.185 246.687 1.00 69.94 ATOM 2949 CE LYS H 63 106.874 121.920 245.230 1.00 60.65 ATOM 2950 NZ LYS H 63 107.680 120.800 244.671 1.00 86.47 ATOM 2951 C LYS H 63 110.106 125.216 247.856 1.00 66.88 ATOM 2952 O LYS H 63 110.361 125.318 246.656 1.00 68.59 ATOM 2953 N PHE H 64 109.740 126.253 248.605 1.00 66.25 ATOM 2954 CA PHE H 64 109.418 127.553 248.010 1.00 67.86 ATOM 2955 CB PHE H 64 107.946 127.890 248.250 1.00 64.87 ATOM 2956 CG PHE H 64 106.992 126.938 247.597 1.00 64.24 ATOM 2957 CD1 PHE H 64 106.330 125.980 248.344 1.00 57.42 ATOM 2958 CE1 PHE H 64 105.447 125.102 247.748 1.00 57.03 ATOM 2959 CZ PHE H 64 105.218 125.174 246.387 1.00 67.21 ATOM 2960 CE2 PHE H 64 105.868 126.126 245.629 1.00 67.94 ATOM 2961 CD2 PHE H 64 106.752 127.002 246.234 1.00 68.36 ATOM 2962 C PHE H 64 110.274 128.708 248.523 1.00 69.32 ATOM 2963 O PHE H 64 110.230 129.809 247.973 1.00 66.02 ATOM 2964 N GLN H 65 111.047 128.454 249.575 1.00 70.24 ATOM 2965 CA GLN H 65 111.784 129.502 250.281 1.00 71.08 ATOM 2966 CB GLN H 65 112.700 128.873 251.335 1.00 73.27 ATOM 2967 CG GLN H 65 113.282 129.865 252.327 1.00 81.77 ATOM 2968 CD GLN H 65 113.867 129.189 253.549 1.00 89.06 ATOM 2969 OE1 GLN H 65 113.854 127.962 253.660 1.00 90.01 ATOM 2970 NE2 GLN H 65 114.383 129.988 254.477 1.00 90.42 ATOM 2971 C GLN H 65 112.587 130.447 249.375 1.00 73.20 ATOM 2972 O GLN H 65 112.715 131.638 249.671 1.00 74.07 ATOM 2973 N ASP H 66 113.113 129.920 248.273 1.00 71.00 ATOM 2974 CA ASP H 66 113.995 130.690 247.400 1.00 72.77 ATOM 2975 CB ASP H 66 114.904 129.751 246.606 1.00 74.93 ATOM 2976 CG ASP H 66 115.059 128.393 247.264 1.00 86.08 ATOM 2977 OD1 ASP H 66 116.205 127.898 247.342 1.00 94.96 ATOM 2978 OD2 ASP H 66 114.034 127.820 247.700 1.00 93.09 ATOM 2979 C ASP H 66 113.230 131.577 246.424 1.00 71.69 ATOM 2980 O ASP H 66 113.778 132.548 245.902 1.00 70.85 ATOM 2981 N ARG H 67 111.967 131.239 246.179 1.00 69.23 ATOM 2982 CA ARG H 67 111.198 131.881 245.118 1.00 68.86 ATOM 2983 CB ARG H 67 110.667 130.833 244.133 1.00 67.15 ATOM 2984 CG ARG H 67 111.492 129.562 244.003 1.00 71.51 ATOM 2985 CD ARG H 67 110.627 128.448 243.420 1.00 60.79 ATOM 2986 NE ARG H 67 109.818 128.960 242.320 1.00 59.06 ATOM 2987 CZ ARG H 67 108.687 128.413 241.884 1.00 61.13 ATOM 2988 NH1 ARG H 67 108.199 127.312 242.447 1.00 48.33 ATOM 2989 NH2 ARG H 67 108.037 128.981 240.875 1.00 58.50 ATOM 2990 C ARG H 67 110.012 132.705 245.626 1.00 68.59 ATOM 2991 O ARG H 67 109.350 133.380 244.838 1.00 69.95 ATOM 2992 N VAL H 68 109.731 132.645 246.926 1.00 67.27 ATOM 2993 CA VAL H 68 108.517 133.268 247.459 1.00 68.14 ATOM 2994 CB VAL H 68 107.585 132.216 248.105 1.00 67.38 ATOM 2995 CG1 VAL H 68 108.078 131.843 249.490 1.00 69.20 ATOM 2996 CG2 VAL H 68 106.160 132.728 248.168 1.00 69.81 ATOM 2997 C VAL H 68 108.795 134.405 248.450 1.00 67.50 ATOM 2998 O VAL H 68 109.747 134.349 249.229 1.00 67.28 ATOM 2999 N THR H 69 107.961 135.440 248.400 1.00 66.11 ATOM 3000 CA THR H 69 108.055 136.568 249.322 1.00 65.18 ATOM 3001 CB THR H 69 108.525 137.846 248.601 1.00 66.85 ATOM 3002 OG1 THR H 69 109.811 137.619 248.014 1.00 69.33 ATOM 3003 CG2 THR H 69 108.631 139.016 249.571 1.00 68.41 ATOM 3004 C THR H 69 106.698 136.829 249.962 1.00 65.68 ATOM 3005 O THR H 69 105.694 136.979 249.265 1.00 66.41 ATOM 3006 N PHE H 70 106.661 136.860 251.289 1.00 64.73 ATOM 3007 CA PHE H 70 105.436 137.205 251.998 1.00 63.08 ATOM 3008 CB PHE H 70 105.178 136.257 253.165 1.00 62.93 ATOM 3009 CG PHE H 70 105.069 134.819 252.761 1.00 62.75 ATOM 3010 CD1 PHE H 70 105.885 133.862 253.336 1.00 63.92 ATOM 3011 CE1 PHE H 70 105.789 132.534 252.964 1.00 64.06 ATOM 3012 CZ PHE H 70 104.879 132.152 252.007 1.00 56.98 ATOM 3013 CE2 PHE H 70 104.057 133.095 251.426 1.00 64.06 ATOM 3014 CD2 PHE H 70 104.156 134.423 251.801 1.00 58.13 ATOM 3015 C PHE H 70 105.537 138.631 252.497 1.00 64.01 ATOM 3016 O PHE H 70 106.605 139.081 252.909 1.00 63.72 ATOM 3017 N THR H 71 104.423 139.347 252.448 1.00 60.83 ATOM 3018 CA THR H 71 104.422 140.746 252.826 1.00 62.37 ATOM 3019 CB THR H 71 104.826 141.627 251.626 1.00 62.78 ATOM 3020 OG1 THR H 71 105.668 142.693 252.072 1.00 71.26 ATOM 3021 CG2 THR H 71 103.609 142.187 250.921 1.00 62.63 ATOM 3022 C THR H 71 103.043 141.124 253.366 1.00 59.72 ATOM 3023 O THR H 71 102.065 140.424 253.107 1.00 56.76 ATOM 3024 N ALA H 72 102.972 142.200 254.143 1.00 56.08 ATOM 3025 CA ALA H 72 101.701 142.639 254.723 1.00 58.20 ATOM 3026 CB ALA H 72 101.507 142.038 256.104 1.00 61.53 ATOM 3027 C ALA H 72 101.595 144.160 254.790 1.00 60.68 ATOM 3028 O ALA H 72 102.587 144.854 255.016 1.00 61.37 ATOM 3029 N ASP H 73 100.391 144.671 254.570 1.00 60.19 ATOM 3030 CA ASP H 73 100.123 146.088 254.746 1.00 61.05 ATOM 3031 CB ASP H 73 99.793 146.753 253.409 1.00 57.87 ATOM 3032 CG ASP H 73 99.576 148.252 253.540 1.00 62.17 ATOM 3033 OD1 ASP H 73 99.564 148.767 254.680 1.00 69.29 ATOM 3034 OD2 ASP H 73 99.415 148.918 252.501 1.00 67.00 ATOM 3035 C ASP H 73 98.971 146.250 255.725 1.00 60.93 ATOM 3036 O ASP H 73 97.804 146.157 255.345 1.00 65.22 ATOM 3037 N THR H 74 99.308 146.489 256.988 1.00 60.98 ATOM 3038 CA THR H 74 98.308 146.594 258.042 1.00 64.19 ATOM 3039 CB THR H 74 98.952 146.744 259.441 1.00 63.75 ATOM 3040 OG1 THR H 74 99.780 147.913 259.470 1.00 72.20 ATOM 3041 CG2 THR H 74 99.790 145.522 259.777 1.00 59.90 ATOM 3042 C THR H 74 97.331 147.741 257.810 1.00 63.15 ATOM 3043 O THR H 74 96.166 147.643 258.181 1.00 67.41 ATOM 3044 N SER H 75 97.800 148.822 257.193 1.00 63.75 ATOM 3045 CA SER H 75 96.932 149.959 256.920 1.00 64.73 ATOM 3046 CB SER H 75 97.744 151.193 256.509 1.00 64.62 ATOM 3047 OG SER H 75 98.134 151.126 255.150 1.00 65.47 ATOM 3048 C SER H 75 95.901 149.617 255.850 1.00 62.14 ATOM 3049 O SER H 75 94.894 150.303 255.713 1.00 65.36 ATOM 3050 N ALA H 76 96.152 148.546 255.103 1.00 63.00 ATOM 3051 CA ALA H 76 95.241 148.109 254.051 1.00 59.36 ATOM 3052 CB ALA H 76 95.983 147.998 252.726 1.00 56.06 ATOM 3053 C ALA H 76 94.554 146.781 254.390 1.00 60.10 ATOM 3054 O ALA H 76 93.790 146.248 253.578 1.00 62.12 ATOM 3055 N ASN H 77 94.822 146.258 255.585 1.00 57.71 ATOM 3056 CA ASN H 77 94.301 144.944 256.013 1.00 62.12 ATOM 3057 CB ASN H 77 92.796 144.994 256.278 1.00 61.03 ATOM 3058 CG ASN H 77 92.430 145.919 257.413 1.00 66.81 ATOM 3059 OD1 ASN H 77 93.160 146.040 258.398 1.00 72.80 ATOM 3060 ND2 ASN H 77 91.285 146.573 257.284 1.00 71.53 ATOM 3061 C ASN H 77 94.569 143.842 255.003 1.00 61.44 ATOM 3062 O ASN H 77 93.732 142.957 254.806 1.00 61.78 ATOM 3063 N THR H 78 95.732 143.894 254.365 1.00 60.91 ATOM 3064 CA THR H 78 96.022 142.997 253.256 1.00 62.04 ATOM 3065 CB THR H 78 95.959 143.754 251.916 1.00 61.25 ATOM 3066 OG1 THR H 78 94.657 144.332 251.765 1.00 63.23 ATOM 3067 CG2 THR H 78 96.215 142.814 250.757 1.00 66.71 ATOM 3068 C THR H 78 97.372 142.296 253.397 1.00 61.76 ATOM 3069 O THR H 78 98.380 142.926 253.707 1.00 59.87 ATOM 3070 N ALA H 79 97.369 140.984 253.189 1.00 62.49 ATOM 3071 CA ALA H 79 98.595 140.213 253.093 1.00 63.03 ATOM 3072 CB ALA H 79 98.487 138.924 253.891 1.00 58.56 ATOM 3073 C ALA H 79 98.848 139.905 251.624 1.00 66.21 ATOM 3074 O ALA H 79 97.912 139.830 250.823 1.00 65.31 ATOM 3075 N TYR H 80 100.117 139.737 251.272 1.00 66.39 ATOM 3076 CA TYR H 80 100.494 139.488 249.896 1.00 65.09 ATOM 3077 CB TYR H 80 101.193 140.705 249.297 1.00 65.21 ATOM 3078 CG TYR H 80 100.394 141.982 249.329 1.00 63.12 ATOM 3079 CD1 TYR H 80 100.495 142.859 250.402 1.00 61.35 ATOM 3080 CE1 TYR H 80 99.773 144.041 250.432 1.00 61.65 ATOM 3081 CZ TYR H 80 98.942 144.356 249.378 1.00 64.01 ATOM 3082 OH TYR H 80 98.220 145.525 249.410 1.00 64.67 ATOM 3083 CE2 TYR H 80 98.829 143.502 248.295 1.00 53.62 ATOM 3084 CD2 TYR H 80 99.555 142.324 248.277 1.00 60.57 ATOM 3085 C TYR H 80 101.435 138.304 249.812 1.00 65.84 ATOM 3086 O TYR H 80 102.266 138.094 250.693 1.00 67.66 ATOM 3087 N MET H 81 101.294 137.536 248.741 1.00 67.10 ATOM 3088 CA MET H 81 102.224 136.471 248.431 1.00 66.08 ATOM 3089 CB MET H 81 101.537 135.112 248.530 1.00 67.65 ATOM 3090 CG MET H 81 102.449 133.912 248.264 1.00 78.02 ATOM 3091 SD MET H 81 102.555 133.456 246.520 1.00 81.98 ATOM 3092 CE MET H 81 100.819 133.236 246.134 1.00 72.54 ATOM 3093 C MET H 81 102.738 136.699 247.022 1.00 65.39 ATOM 3094 O MET H 81 101.959 136.797 246.077 1.00 62.11 ATOM 3095 N GLU H 82 104.051 136.808 246.881 1.00 62.88 ATOM 3096 CA GLU H 82 104.632 136.895 245.557 1.00 64.78 ATOM 3097 CB GLU H 82 105.454 138.170 245.383 1.00 62.80 ATOM 3098 CG GLU H 82 105.895 138.373 243.950 1.00 66.59 ATOM 3099 CD GLU H 82 106.770 139.587 243.767 1.00 79.35 ATOM 3100 OE1 GLU H 82 106.618 140.274 242.734 1.00 85.23 ATOM 3101 OE2 GLU H 82 107.610 139.853 244.652 1.00 84.37 ATOM 3102 C GLU H 82 105.485 135.670 245.266 1.00 61.58 ATOM 3103 O GLU H 82 106.342 135.293 246.064 1.00 65.25 ATOM 3104 N LEU H 83 105.236 135.050 244.119 1.00 59.91 ATOM 3105 CA LEU H 83 106.005 133.891 243.689 1.00 58.18 ATOM 3106 CB LEU H 83 105.078 132.686 243.518 1.00 56.51 ATOM 3107 CG LEU H 83 105.687 131.313 243.229 1.00 61.66 ATOM 3108 CD1 LEU H 83 106.641 130.897 244.336 1.00 48.61 ATOM 3109 CD2 LEU H 83 104.586 130.276 243.045 1.00 54.59 ATOM 3110 C LEU H 83 106.711 134.211 242.375 1.00 58.52 ATOM 3111 O LEU H 83 106.060 134.531 241.384 1.00 57.76 ATOM 3112 N ARG H 84 108.039 134.126 242.363 1.00 59.60 ATOM 3113 CA ARG H 84 108.794 134.429 241.147 1.00 61.46 ATOM 3114 CB ARG H 84 109.869 135.488 241.418 1.00 63.72 ATOM 3115 CG ARG H 84 110.875 135.120 242.493 1.00 70.26 ATOM 3116 CD ARG H 84 111.710 136.330 242.903 1.00 79.20 ATOM 3117 NE ARG H 84 112.376 136.112 244.184 1.00 83.42 ATOM 3118 CZ ARG H 84 111.762 136.166 245.364 1.00 91.74 ATOM 3119 NH1 ARG H 84 112.449 135.950 246.480 1.00 94.14 ATOM 3120 NH2 ARG H 84 110.460 136.432 245.431 1.00 87.19 ATOM 3121 C ARG H 84 109.389 133.185 240.479 1.00 61.20 ATOM 3122 O ARG H 84 109.225 132.065 240.972 1.00 60.06 ATOM 3123 N SER H 85 110.069 133.400 239.352 1.00 59.69 ATOM 3124 CA SER H 85 110.600 132.315 238.521 1.00 60.15 ATOM 3125 CB SER H 85 111.846 131.695 239.159 1.00 59.68 ATOM 3126 OG SER H 85 112.196 130.486 238.508 1.00 69.42 ATOM 3127 C SER H 85 109.546 131.240 238.234 1.00 58.26 ATOM 3128 O SER H 85 109.818 130.040 238.327 1.00 52.83 ATOM 3129 N LEU H 86 108.346 131.683 237.871 1.00 58.22 ATOM 3130 CA LEU H 86 107.216 130.781 237.687 1.00 57.38 ATOM 3131 CB LEU H 86 105.956 131.561 237.321 1.00 57.45 ATOM 3132 CG LEU H 86 105.334 132.406 238.429 1.00 55.99 ATOM 3133 CD1 LEU H 86 104.386 133.427 237.824 1.00 61.32 ATOM 3134 CD2 LEU H 86 104.619 131.514 239.434 1.00 54.74 ATOM 3135 C LEU H 86 107.487 129.722 236.632 1.00 59.69 ATOM 3136 O LEU H 86 108.257 129.936 235.701 1.00 57.92 ATOM 3137 N ARG H 87 106.838 128.577 236.791 1.00 60.95 ATOM 3138 CA ARG H 87 106.972 127.472 235.860 1.00 61.82 ATOM 3139 CB ARG H 87 107.943 126.423 236.410 1.00 59.17 ATOM 3140 CG ARG H 87 107.545 125.873 237.772 1.00 72.01 ATOM 3141 CD ARG H 87 108.743 125.339 238.546 1.00 74.52 ATOM 3142 NE ARG H 87 109.779 126.354 238.715 1.00 80.41 ATOM 3143 CZ ARG H 87 110.747 126.298 239.627 1.00 87.15 ATOM 3144 NH1 ARG H 87 110.811 125.274 240.473 1.00 88.38 ATOM 3145 NH2 ARG H 87 111.650 127.269 239.699 1.00 79.79 ATOM 3146 C ARG H 87 105.584 126.889 235.675 1.00 62.31 ATOM 3147 O ARG H 87 104.681 127.185 236.457 1.00 60.76 ATOM 3148 N SER H 88 105.400 126.074 234.644 1.00 62.62 ATOM 3149 CA SER H 88 104.069 125.588 234.320 1.00 65.38 ATOM 3150 CB SER H 88 104.095 124.710 233.066 1.00 65.60 ATOM 3151 OG SER H 88 104.307 123.355 233.408 1.00 71.88 ATOM 3152 C SER H 88 103.476 124.833 235.509 1.00 66.15 ATOM 3153 O SER H 88 102.265 124.868 235.737 1.00 65.91 ATOM 3154 N ALA H 89 104.339 124.173 236.278 1.00 64.83 ATOM 3155 CA ALA H 89 103.904 123.408 237.440 1.00 60.52 ATOM 3156 CB ALA H 89 105.032 122.518 237.927 1.00 62.85 ATOM 3157 C ALA H 89 103.388 124.293 238.579 1.00 60.18 ATOM 3158 O ALA H 89 102.847 123.798 239.565 1.00 63.17 ATOM 3159 N ASP H 90 103.561 125.602 238.449 1.00 60.25 ATOM 3160 CA ASP H 90 103.080 126.529 239.467 1.00 56.39 ATOM 3161 CB ASP H 90 103.917 127.808 239.490 1.00 54.73 ATOM 3162 CG ASP H 90 105.294 127.596 240.080 1.00 61.34 ATOM 3163 OD1 ASP H 90 105.451 126.699 240.937 1.00 61.95 ATOM 3164 OD2 ASP H 90 106.223 128.332 239.687 1.00 63.28 ATOM 3165 C ASP H 90 101.625 126.873 239.207 1.00 57.86 ATOM 3166 O ASP H 90 101.012 127.631 239.961 1.00 57.01 ATOM 3167 N THR H 91 101.080 126.323 238.126 1.00 58.12 ATOM 3168 CA THR H 91 99.670 126.501 237.815 1.00 59.15 ATOM 3169 CB THR H 91 99.303 125.879 236.457 1.00 57.07 ATOM 3170 OG1 THR H 91 99.909 126.647 235.408 1.00 58.32 ATOM 3171 CG2 THR H 91 97.781 125.864 236.254 1.00 56.05 ATOM 3172 C THR H 91 98.829 125.873 238.919 1.00 61.64 ATOM 3173 O THR H 91 98.848 124.661 239.111 1.00 64.64 ATOM 3174 N ALA H 92 98.105 126.708 239.653 1.00 60.28 ATOM 3175 CA ALA H 92 97.343 126.237 240.793 1.00 58.81 ATOM 3176 CB ALA H 92 98.281 125.852 241.924 1.00 62.00 ATOM 3177 C ALA H 92 96.353 127.279 241.278 1.00 60.65 ATOM 3178 O ALA H 92 96.349 128.418 240.811 1.00 58.69 ATOM 3179 N VAL H 93 95.500 126.861 242.209 1.00 61.24 ATOM 3180 CA VAL H 93 94.701 127.786 242.981 1.00 61.62 ATOM 3181 CB VAL H 93 93.323 127.192 243.335 1.00 62.71 ATOM 3182 CG1 VAL H 93 92.498 128.212 244.101 1.00 54.78 ATOM 3183 CG2 VAL H 93 92.591 126.755 242.066 1.00 55.47 ATOM 3184 C VAL H 93 95.480 128.103 244.252 1.00 58.03 ATOM 3185 O VAL H 93 95.864 127.203 244.983 1.00 57.31 ATOM 3186 N TYR H 94 95.732 129.386 244.486 1.00 62.44 ATOM 3187 CA TYR H 94 96.489 129.844 245.648 1.00 60.73 ATOM 3188 CB TYR H 94 97.543 130.867 245.211 1.00 63.40 ATOM 3189 CG TYR H 94 98.674 130.243 244.416 1.00 61.43 ATOM 3190 CD1 TYR H 94 98.508 129.889 243.081 1.00 62.11 ATOM 3191 CE1 TYR H 94 99.544 129.298 242.363 1.00 61.11 ATOM 3192 CZ TYR H 94 100.753 129.055 242.993 1.00 60.40 ATOM 3193 OH TYR H 94 101.802 128.472 242.314 1.00 58.98 ATOM 3194 CE2 TYR H 94 100.931 129.397 244.312 1.00 57.86 ATOM 3195 CD2 TYR H 94 99.899 129.979 245.014 1.00 62.14 ATOM 3196 C TYR H 94 95.555 130.424 246.715 1.00 64.91 ATOM 3197 O TYR H 94 94.780 131.345 246.449 1.00 62.46 ATOM 3198 N TYR H 95 95.634 129.867 247.919 1.00 60.34 ATOM 3199 CA TYR H 95 94.733 130.210 249.002 1.00 56.09 ATOM 3200 CB TYR H 95 94.125 128.942 249.594 1.00 54.97 ATOM 3201 CG TYR H 95 93.246 128.127 248.680 1.00 56.93 ATOM 3202 CD1 TYR H 95 91.878 128.367 248.607 1.00 54.63 ATOM 3203 CE1 TYR H 95 91.057 127.606 247.795 1.00 60.03 ATOM 3204 CZ TYR H 95 91.600 126.585 247.043 1.00 62.06 ATOM 3205 OH TYR H 95 90.781 125.825 246.233 1.00 59.27 ATOM 3206 CE2 TYR H 95 92.955 126.321 247.099 1.00 56.88 ATOM 3207 CD2 TYR H 95 93.771 127.089 247.919 1.00 58.85 ATOM 3208 C TYR H 95 95.480 130.886 250.131 1.00 61.29 ATOM 3209 O TYR H 95 96.557 130.431 250.522 1.00 62.10 ATOM 3210 N CYS H 96 94.906 131.955 250.679 1.00 59.33 ATOM 3211 CA CYS H 96 95.355 132.444 251.979 1.00 58.25 ATOM 3212 CB CYS H 96 95.417 133.973 252.015 1.00 57.87 ATOM 3213 SG CYS H 96 93.828 134.784 251.758 1.00 66.42 ATOM 3214 C CYS H 96 94.394 131.907 253.040 1.00 61.76 ATOM 3215 O CYS H 96 93.237 131.591 252.743 1.00 63.30 ATOM 3216 N ALA H 97 94.871 131.800 254.272 1.00 58.82 ATOM 3217 CA ALA H 97 94.034 131.344 255.375 1.00 63.13 ATOM 3218 CB ALA H 97 93.960 129.815 255.409 1.00 55.23 ATOM 3219 C ALA H 97 94.579 131.878 256.691 1.00 62.21 ATOM 3220 O ALA H 97 95.789 131.914 256.898 1.00 63.85 ATOM 3221 N ARG H 98 93.675 132.288 257.574 1.00 62.93 ATOM 3222 CA ARG H 98 94.040 132.805 258.884 1.00 60.92 ATOM 3223 CB ARG H 98 92.957 133.764 259.370 1.00 61.53 ATOM 3224 CG ARG H 98 93.397 134.652 260.522 1.00 64.67 ATOM 3225 CD ARG H 98 92.211 135.243 261.252 1.00 63.28 ATOM 3226 NE ARG H 98 91.518 134.245 262.056 1.00 58.83 ATOM 3227 CZ ARG H 98 90.554 134.532 262.921 1.00 65.79 ATOM 3228 NH1 ARG H 98 90.176 135.793 263.102 1.00 56.86 ATOM 3229 NH2 ARG H 98 89.976 133.563 263.613 1.00 58.03 ATOM 3230 C ARG H 98 94.187 131.674 259.901 1.00 63.33 ATOM 3231 O ARG H 98 93.415 130.712 259.883 1.00 62.20 ATOM 3232 N VAL H 99 95.164 131.791 260.802 1.00 61.66 ATOM 3233 CA VAL H 99 95.260 130.844 261.905 1.00 58.70 ATOM 3234 CB VAL H 99 96.595 130.960 262.679 1.00 58.77 ATOM 3235 CG1 VAL H 99 97.776 130.636 261.755 1.00 51.91 ATOM 3236 CG2 VAL H 99 96.749 132.349 263.342 1.00 56.17 ATOM 3237 C VAL H 99 94.054 131.024 262.840 1.00 60.50 ATOM 3238 O VAL H 99 93.333 132.013 262.743 1.00 61.51 ATOM 3239 N GLY H 100 93.815 130.054 263.716 1.00 57.58 ATOM 3240 CA GLY H 100 92.747 130.183 264.698 1.00 56.69 ATOM 3241 C GLY H 100 93.168 131.054 265.870 1.00 61.19 ATOM 3242 O GLY H 100 94.334 131.455 265.963 1.00 58.59 ATOM 3243 N PRO H 101 92.221 131.360 266.773 1.00 58.97 ATOM 3244 CA PRO H 101 92.543 132.154 267.957 1.00 61.76 ATOM 3245 CB PRO H 101 91.173 132.419 268.586 1.00 61.11 ATOM 3246 CG PRO H 101 90.315 131.276 268.109 1.00 62.44 ATOM 3247 CD PRO H 101 90.801 130.972 266.728 1.00 56.04 ATOM 3248 C PRO H 101 93.426 131.383 268.934 1.00 63.94 ATOM 3249 O PRO H 101 93.228 130.179 269.137 1.00 62.02 ATOM 3250 N TYR H 102 94.398 132.074 269.522 1.00 61.94 ATOM 3251 CA TYR H 102 95.223 131.489 270.574 1.00 60.03 ATOM 3252 CB TYR H 102 96.632 132.082 270.570 1.00 55.44 ATOM 3253 CG TYR H 102 97.471 131.613 271.734 1.00 58.46 ATOM 3254 CD1 TYR H 102 97.522 132.333 272.922 1.00 68.53 ATOM 3255 CE1 TYR H 102 98.280 131.892 273.993 1.00 62.79 ATOM 3256 CZ TYR H 102 99.000 130.720 273.877 1.00 63.96 ATOM 3257 OH TYR H 102 99.766 130.261 274.929 1.00 62.37 ATOM 3258 CE2 TYR H 102 98.962 129.995 272.709 1.00 63.87 ATOM 3259 CD2 TYR H 102 98.204 130.439 271.651 1.00 60.24 ATOM 3260 C TYR H 102 94.596 131.713 271.945 1.00 61.88 ATOM 3261 O TYR H 102 94.073 132.795 272.237 1.00 62.36 ATOM 3262 N SER H 103 94.679 130.692 272.791 1.00 56.96 ATOM 3263 CA SER H 103 94.169 130.773 274.148 1.00 62.33 ATOM 3264 CB SER H 103 92.963 129.843 274.306 1.00 63.46 ATOM 3265 OG SER H 103 92.586 129.729 275.667 1.00 84.73 ATOM 3266 C SER H 103 95.260 130.390 275.143 1.00 61.30 ATOM 3267 O SER H 103 96.194 129.668 274.807 1.00 63.77 ATOM 3268 N TRP H 104 95.127 130.870 276.373 1.00 62.42 ATOM 3269 CA TRP H 104 96.091 130.592 277.431 1.00 60.71 ATOM 3270 CB TRP H 104 95.547 131.128 278.749 1.00 56.60 ATOM 3271 CG TRP H 104 96.447 130.963 279.922 1.00 62.98 ATOM 3272 CD1 TRP H 104 96.257 130.128 280.991 1.00 59.55 ATOM 3273 NE1 TRP H 104 97.289 130.268 281.888 1.00 63.95 ATOM 3274 CE2 TRP H 104 98.176 131.195 281.407 1.00 61.82 ATOM 3275 CD2 TRP H 104 97.675 131.661 280.172 1.00 56.03 ATOM 3276 CE3 TRP H 104 98.404 132.625 279.469 1.00 55.19 ATOM 3277 CZ3 TRP H 104 99.592 133.089 280.014 1.00 59.29 ATOM 3278 CH2 TRP H 104 100.059 132.617 281.247 1.00 57.30 ATOM 3279 CZ2 TRP H 104 99.371 131.668 281.956 1.00 65.92 ATOM 3280 C TRP H 104 96.435 129.103 277.560 1.00 61.85 ATOM 3281 O TRP H 104 97.594 128.746 277.754 1.00 64.86 ATOM 3282 N ASP H 105 95.431 128.240 277.441 1.00 63.21 ATOM 3283 CA ASP H 105 95.620 126.798 277.620 1.00 63.56 ATOM 3284 CB ASP H 105 94.272 126.106 277.827 1.00 63.94 ATOM 3285 CG ASP H 105 93.635 126.460 279.154 1.00 72.27 ATOM 3286 OD1 ASP H 105 92.512 125.981 279.422 1.00 84.18 ATOM 3287 OD2 ASP H 105 94.256 127.212 279.933 1.00 67.38 ATOM 3288 C ASP H 105 96.359 126.121 276.468 1.00 66.44 ATOM 3289 O ASP H 105 96.757 124.962 276.580 1.00 70.81 ATOM 3290 N ASP H 106 96.527 126.834 275.359 1.00 67.25 ATOM 3291 CA ASP H 106 97.229 126.288 274.199 1.00 68.65 ATOM 3292 CB ASP H 106 96.858 127.057 272.925 1.00 68.25 ATOM 3293 CG ASP H 106 95.384 126.993 272.603 1.00 71.95 ATOM 3294 OD1 ASP H 106 94.753 125.950 272.872 1.00 69.08 ATOM 3295 OD2 ASP H 106 94.859 127.990 272.065 1.00 75.65 ATOM 3296 C ASP H 106 98.739 126.379 274.364 1.00 66.83 ATOM 3297 O ASP H 106 99.250 127.266 275.054 1.00 65.89 ATOM 3298 N SER H 107 99.443 125.461 273.712 1.00 62.29 ATOM 3299 CA SER H 107 100.867 125.622 273.465 1.00 65.58 ATOM 3300 CB SER H 107 101.530 124.266 273.223 1.00 61.40 ATOM 3301 OG SER H 107 101.390 123.425 274.355 1.00 73.26 ATOM 3302 C SER H 107 101.010 126.493 272.225 1.00 63.68 ATOM 3303 O SER H 107 100.145 126.470 271.350 1.00 64.78 ATOM 3304 N PRO H 108 102.093 127.278 272.149 1.00 62.96 ATOM 3305 CA PRO H 108 102.332 128.076 270.953 1.00 63.21 ATOM 3306 CB PRO H 108 103.796 128.496 271.109 1.00 65.22 ATOM 3307 CG PRO H 108 103.992 128.578 272.585 1.00 60.50 ATOM 3308 CD PRO H 108 103.141 127.473 273.168 1.00 60.97 ATOM 3309 C PRO H 108 102.134 127.259 269.671 1.00 63.11 ATOM 3310 O PRO H 108 102.685 126.170 269.542 1.00 63.17 ATOM 3311 N GLN H 109 101.330 127.786 268.747 1.00 63.73 ATOM 3312 CA GLN H 109 101.091 127.158 267.440 1.00 62.55 ATOM 3313 CB GLN H 109 102.407 126.716 266.783 1.00 63.82 ATOM 3314 CG GLN H 109 103.359 227.868 266.505 1.00 66.48 ATOM 3315 CD GLN H 109 104.404 127.536 265.462 1.00 68.95 ATOM 3316 OE1 GLN H 109 104.533 126.392 265.034 1.00 68.12 ATOM 3317 NE2 GLN H 109 105.158 128.542 265.048 1.00 66.34 ATOM 3318 C GLN H 109 100.072 126.017 267.449 1.00 62.47 ATOM 3319 O GLN H 109 99.823 125.394 266.414 1.00 60.33 ATOM 3320 N ASP H 110 99.479 125.739 268.606 1.00 58.61 ATOM 3321 CA ASP H 110 98.360 124.802 268.649 1.00 61.51 ATOM 3322 CB ASP H 110 97.841 124.630 270.075 1.00 58.46 ATOM 3323 CG ASP H 110 98.643 123.618 270.879 1.00 64.16 ATOM 3324 OD1 ASP H 110 98.346 123.467 272.085 1.00 61.26 ATOM 3325 OD2 ASP H 110 99.559 122.975 270.314 1.00 59.50 ATOM 3326 C ASP H 110 97.233 125.315 267.751 1.00 59.87 ATOM 3327 O ASP H 110 96.418 124.538 267.243 1.00 61.48 ATOM 3328 N ASN H 111 97.208 126.629 267.557 1.00 60.04 ATOM 3329 CA ASN H 111 96.163 127.294 266.783 1.00 62.68 ATOM 3330 CB ASN H 111 95.837 128.647 267.417 1.00 61.45 ATOM 3331 CG ASN H 111 97.033 129.569 267.445 1.00 62.28 ATOM 3332 OD1 ASN H 111 98.065 129.236 268.019 1.00 63.37 ATOM 3333 ND2 ASN H 111 96.906 130.733 266.816 1.00 61.03 ATOM 3334 C ASN H 111 96.516 127.526 265.314 1.00 61.65 ATOM 3335 O ASN H 111 95.748 128.163 264.592 1.00 63.55 ATOM 3336 N TYR H 112 97.672 127.028 264.874 1.00 59.75 ATOM 3337 CA TYR H 112 98.160 127.327 263.521 1.00 59.79 ATOM 3338 CB TYR H 112 99.690 127.238 263.452 1.00 59.70 ATOM 3339 CG TYR H 112 100.420 128.518 263.829 1.00 62.39 ATOM 3340 CD1 TYR H 112 99.934 129.356 264.824 1.00 60.35 ATOM 3341 CE1 TYR H 112 100.610 130.514 265.183 1.00 60.73 ATOM 3342 CZ TYR H 112 101.790 130.844 264.539 1.00 65.84 ATOM 3343 OH TYR H 112 102.469 131.990 264.891 1.00 60.50 ATOM 3344 CE2 TYR H 112 102.293 130.029 263.551 1.00 64.34 ATOM 3345 CD2 TYR H 112 101.611 128.870 263.204 1.00 66.77 ATOM 3346 C TYR H 112 97.527 126.455 262.444 1.00 59.14 ATOM 3347 O TYR H 112 98.131 126.198 261.400 1.00 62.33 ATOM 3348 N TYR H 113 96.318 125.975 262.704 1.00 57.97 ATOM 3349 CA TYR H 113 95.559 125.292 261.674 1.00 58.85 ATOM 3350 CB TYR H 113 94.457 124.419 262.287 1.00 62.21 ATOM 3351 CG TYR H 113 93.660 125.116 263.366 1.00 63.70 ATOM 3352 CD1 TYR H 113 93.970 124.941 264.713 1.00 59.66 ATOM 3353 CE1 TYR H 113 93.250 125.584 265.700 1.00 58.25 ATOM 3354 CZ TYR H 113 92.208 126.415 265.347 1.00 58.34 ATOM 3355 OH TYR H 113 91.478 127.053 266.316 1.00 66.79 ATOM 3356 CE2 TYR H 113 91.879 126.604 264.022 1.00 54.53 ATOM 3357 CD2 TYR H 113 92.603 125.956 263.039 1.00 59.51 ATOM 3358 C TYR H 113 94.984 126.367 260.761 1.00 58.21 ATOM 3359 O TYR H 113 95.256 127.555 260.950 1.00 57.86 ATOM 3360 N MET H 114 94.212 125.961 259.758 1.00 58.91 ATOM 3361 CA MET H 114 93.664 126.926 258.809 1.00 62.31 ATOM 3362 CB MET H 114 93.840 126.444 257.372 1.00 66.20 ATOM 3363 CG MET H 114 95.079 127.026 256.697 1.00 77.46 ATOM 3364 SD MET H 114 96.495 125.936 256.506 1.00 95.80 ATOM 3365 CE MET H 114 96.980 125.560 258.194 1.00 57.46 ATOM 3366 C MET H 114 92.206 127.225 259.133 1.00 62.25 ATOM 3367 O MET H 114 91.293 126.533 258.677 1.00 58.57 ATOM 3368 N ASP H 115 92.012 128.264 259.937 1.00 58.06 ATOM 3369 CA ASP H 115 90.732 128.537 260.567 1.00 59.82 ATOM 3370 CB ASP H 115 90.934 129.510 261.731 1.00 56.39 ATOM 3371 CG ASP H 115 89.740 129.582 262.638 1.00 58.31 ATOM 3372 OD1 ASP H 115 88.973 128.603 262.662 1.00 65.63 ATOM 3373 OD2 ASP H 115 89.569 130.612 263.332 1.00 62.51 ATOM 3374 C ASP H 115 89.720 129.099 259.578 1.00 61.88 ATOM 3375 O ASP H 115 88.565 128.680 259.560 1.00 63.09 ATOM 3376 N VAL H 116 90.163 130.056 258.769 1.00 59.64 ATOM 3377 CA VAL H 116 89.308 130.690 257.775 1.00 61.47 ATOM 3378 CB VAL H 116 88.892 132.111 258.202 1.00 66.10 ATOM 3379 CG1 VAL H 116 88.063 132.775 257.107 1.00 61.02 ATOM 3380 CG2 VAL H 116 88.122 132.074 259.513 1.00 63.28 ATOM 3381 C VAL H 116 90.072 130.797 256.470 1.00 61.35 ATOM 3382 O VAL H 116 91.181 131.338 256.434 1.00 62.34 ATOM 3383 N TRP H 117 89.485 130.277 255.398 1.00 59.18 ATOM 3384 CA TRP H 117 90.148 130.285 254.100 1.00 61.87 ATOM 3385 CB TRP H 117 89.982 128.939 253.397 1.00 60.78 ATOM 3386 CG TRP H 117 90.600 127.747 254.058 1.00 66.03 ATOM 3387 CD1 TRP H 117 90.245 127.187 255.260 1.00 60.65 ATOM 3388 NE1 TRP H 117 91.016 126.075 255.505 1.00 58.71 ATOM 3389 CE2 TRP H 117 91.876 125.885 254.452 1.00 62.94 ATOM 3390 CD2 TRP H 117 91.642 126.920 253.520 1.00 59.50 ATOM 3391 CE3 TRP H 117 92.397 126.953 252.340 1.00 62.18 ATOM 3392 CZ3 TRP H 117 93.360 125.974 252.134 1.00 60.59 ATOM 3393 CH2 TRP H 117 93.577 124.959 253.085 1.00 61.14 ATOM 3394 CZ2 TRP H 117 92.849 124.898 254.245 1.00 54.60 ATOM 3395 C TRP H 117 89.562 131.342 253.188 1.00 58.03 ATOM 3396 O TRP H 117 88.369 131.652 253.260 1.00 61.32 ATOM 3397 N GLY H 118 90.400 131.880 252.308 1.00 62.13 ATOM 3398 CA GLY H 118 89.908 132.645 251.172 1.00 57.19 ATOM 3399 C GLY H 118 89.374 131.675 250.131 1.00 62.39 ATOM 3400 O GLY H 118 89.619 130.467 250.216 1.00 58.89 ATOM 3401 N LYS H 119 88.639 132.188 249.148 1.00 62.35 ATOM 3402 CA LYS H 119 88.103 131.334 248.090 1.00 65.59 ATOM 3403 CB LYS H 119 86.939 132.015 247.365 1.00 65.25 ATOM 3404 CG LYS H 119 85.710 132.251 248.248 1.00 68.61 ATOM 3405 CD LYS H 119 84.429 132.228 247.426 1.00 84.49 ATOM 3406 CE LYS H 119 84.110 133.584 246.823 1.00 100.11 ATOM 3407 NZ LYS H 119 83.349 134.450 247.774 1.00 101.29 ATOM 3408 C LYS H 119 89.187 130.907 247.096 1.00 64.39 ATOM 3409 O LYS H 119 88.957 130.052 246.244 1.00 66.77 ATOM 3410 N GLY H 120 90.366 131.505 247.214 1.00 63.74 ATOM 3411 CA GLY H 120 91.488 131.169 246.341 1.00 63.72 ATOM 3412 C GLY H 120 91.577 132.035 245.102 1.00 63.84 ATOM 3413 O GLY H 120 90.599 132.682 244.713 1.00 58.89 ATOM 3414 N THR H 121 92.759 132.063 244.489 1.00 62.47 ATOM 3415 CA THR H 121 92.936 132.726 243.202 1.00 63.56 ATOM 3416 CB THR H 121 93.651 134.107 243.307 1.00 67.68 ATOM 3417 OG1 THR H 121 94.982 134.017 242.784 1.00 73.82 ATOM 3418 CG2 THR H 121 93.687 134.611 244.727 1.00 57.10 ATOM 3419 C THR H 121 93.705 131.830 242.241 1.00 61.01 ATOM 3420 O THR H 121 94.775 131.327 242.566 1.00 63.37 ATOM 3421 N THR H 122 93.141 131.635 241.056 1.00 62.98 ATOM 3422 CA THR H 122 93.750 130.796 240.032 1.00 60.76 ATOM 3423 CB THR H 122 92.716 130.440 238.942 1.00 64.15 ATOM 3424 OG1 THR H 122 91.678 129.638 239.520 1.00 63.03 ATOM 3425 CG2 THR H 122 93.369 129.680 237.767 1.00 55.41 ATOM 3426 C THR H 122 94.946 131.493 239.393 1.00 63.14 ATOM 3427 O THR H 122 94.832 132.609 238.881 1.00 58.61 ATOM 3428 N VAL H 123 96.101 130.842 239.445 1.00 60.83 ATOM 3429 CA VAL H 123 97.261 131.326 238.709 1.00 59.32 ATOM 3430 CB VAL H 123 98.485 131.567 239.611 1.00 58.18 ATOM 3431 CG1 VAL H 123 99.685 131.981 238.777 1.00 59.39 ATOM 3432 CG2 VAL H 123 98.174 132.634 240.657 1.00 57.40 ATOM 3433 C VAL H 123 97.606 130.325 237.621 1.00 60.69 ATOM 3434 O VAL H 123 97.851 129.148 237.892 1.00 62.13 ATOM 3435 N ILE H 124 97.600 130.804 236.385 1.00 62.53 ATOM 3436 CA ILE H 124 97.937 129.984 235.239 1.00 61.86 ATOM 3437 CB ILE H 124 96.899 130.154 234.117 1.00 61.17 ATOM 3438 CG1 ILE H 124 95.524 129.684 234.603 1.00 67.59 ATOM 3439 CD1 ILE H 124 94.420 129.881 233.576 1.00 92.53 ATOM 3440 CG2 ILE H 124 97.320 129.380 232.876 1.00 48.87 ATOM 3441 C ILE H 124 99.315 130.378 234.733 1.00 61.10 ATOM 3442 O ILE H 124 99.573 131.548 234.457 1.00 61.23 ATOM 3443 N VAL H 125 100.211 129.404 234.644 1.00 60.00 ATOM 3444 CA VAL H 125 101.530 129.650 234.085 1.00 57.57 ATOM 3445 CB VAL H 125 102.657 129.249 235.042 1.00 56.78 ATOM 3446 CG1 VAL H 125 104.005 129.583 234.419 1.00 49.76 ATOM 3447 CG2 VAL H 125 102.492 129.964 236.376 1.00 59.06 ATOM 3448 C VAL H 125 101.667 128.891 232.780 1.00 56.12 ATOM 3449 O VAL H 125 101.613 127.662 232.756 1.00 59.91 ATOM 3450 N SER H 126 101.845 129.638 231.696 1.00 53.98 ATOM 3451 CA SER H 126 101.833 129.069 230.364 1.00 53.69 ATOM 3452 CB SER H 126 100.395 128.755 229.946 1.00 52.34 ATOM 3453 OG SER H 126 100.338 128.277 228.615 1.00 55.46 ATOM 3454 C SER H 126 102.447 130.051 229.385 1.00 55.11 ATOM 3455 O SER H 126 102.336 131.270 229.562 1.00 56.24 ATOM 3456 N SER H 127 103.096 129.511 228.356 1.00 55.52 ATOM 3457 CA SER H 127 103.688 130.316 227.288 1.00 51.80 ATOM 3458 CB SER H 127 104.856 129.568 226.635 1.00 52.61 ATOM 3459 OG SER H 127 106.105 129.989 227.161 1.00 61.28 ATOM 3460 C SER H 127 102.651 130.678 226.229 1.00 50.06 ATOM 3461 O SER H 127 102.900 131.520 225.364 1.00 49.55 ATOM 3462 N ALA H 128 101.493 130.030 226.295 1.00 52.02 ATOM 3463 CA ALA H 128 100.417 130.296 225.352 1.00 53.53 ATOM 3464 CB ALA H 128 99.271 129.324 225.566 1.00 53.93 ATOM 3465 C ALA H 128 99.923 131.730 225.478 1.00 52.32 ATOM 3466 O ALA H 128 99.887 132.292 226.570 1.00 56.66 ATOM 3467 N SER H 129 99.552 132.324 224.352 1.00 52.90 ATOM 3468 CA SER H 129 98.924 133.636 224.375 1.00 56.63 ATOM 3469 CB SER H 129 99.570 134.586 223.364 1.00 56.44 ATOM 3470 OG SER H 129 99.932 133.910 222.177 1.00 69.03 ATOM 3471 C SER H 129 97.435 133.484 224.122 1.00 57.06 ATOM 3472 O SER H 129 96.973 132.413 223.733 1.00 58.06 ATOM 3473 N THR H 130 96.687 134.554 224.364 1.00 62.30 ATOM 3474 CA THR H 130 95.237 134.519 224.255 1.00 60.40 ATOM 3475 CB THR H 130 94.630 135.902 224.505 1.00 60.06 ATOM 3476 OG1 THR H 130 95.089 136.387 225.771 1.00 65.20 ATOM 3477 CG2 THR H 130 93.111 135.822 224.533 1.00 56.29 ATOM 3478 C THR H 130 94.803 133.990 222.899 1.00 61.31 ATOM 3479 O THR H 130 95.313 134.405 221.859 1.00 60.65 ATOM 3480 N LYS H 131 93.856 133.065 222.921 1.00 63.15 ATOM 3481 CA LYS H 131 93.428 132.381 221.717 1.00 59.85 ATOM 3482 CB LYS H 131 94.164 131.042 221.621 1.00 61.44 ATOM 3483 CG LYS H 131 94.491 130.553 220.220 1.00 64.98 ATOM 3484 CD LYS H 131 93.248 130.167 219.454 1.00 75.95 ATOM 3485 CE LYS H 131 93.541 129.095 218.420 1.00 67.39 ATOM 3486 NZ LYS H 131 92.284 128.652 217.768 1.00 71.29 ATOM 3487 C LYS H 131 91.927 132.148 221.839 1.00 61.48 ATOM 3488 O LYS H 131 91.466 131.565 222.819 1.00 59.43 ATOM 3489 N GLY H 132 91.163 132.631 220.864 1.00 61.64 ATOM 3490 CA GLY H 132 89.721 132.391 220.834 1.00 58.85 ATOM 3491 C GLY H 132 89.460 131.014 220.252 1.00 62.96 ATOM 3492 O GLY H 132 90.244 130.522 219.443 1.00 62.68 ATOM 3493 N PRO H 133 88.355 130.377 220.656 1.00 62.46 ATOM 3494 CA PRO H 133 88.104 129.004 220.244 1.00 61.77 ATOM 3495 CB PRO H 133 87.110 128.517 221.296 1.00 63.73 ATOM 3496 CG PRO H 133 86.324 129.738 221.635 1.00 62.91 ATOM 3497 CD PRO H 133 87.282 130.901 221.521 1.00 63.33 ATOM 3498 C PRO H 133 87.466 128.894 218.870 1.00 60.36 ATOM 3499 O PRO H 133 86.813 129.831 218.411 1.00 58.44 ATOM 3500 N SER H 134 87.667 127.750 218.222 1.00 61.14 ATOM 3501 CA SER H 134 86.860 127.358 217.077 1.00 59.48 ATOM 3502 CB SER H 134 87.667 126.472 216.131 1.00 61.48 ATOM 3503 OG SER H 134 88.671 127.210 215.452 1.00 64.14 ATOM 3504 C SER H 134 85.672 126.576 217.628 1.00 63.82 ATOM 3505 O SER H 134 85.830 125.797 218.567 1.00 66.74 ATOM 3506 N VAL H 135 84.482 126.799 217.072 1.00 64.67 ATOM 3507 CA VAL H 135 83.280 126.104 217.542 1.00 61.24 ATOM 3508 CB VAL H 135 82.193 127.088 218.025 1.00 65.26 ATOM 3509 CG1 VAL H 135 81.047 126.336 218.703 1.00 59.12 ATOM 3510 CG2 VAL H 135 82.789 128.112 218.981 1.00 63.37 ATOM 3511 C VAL H 135 82.716 125.212 216.444 1.00 63.63 ATOM 3512 O VAL H 135 82.304 125.693 215.383 1.00 63.94 ATOM 3513 N PHE H 136 82.713 123.906 216.699 1.00 61.82 ATOM 3514 CA PHE H 136 82.253 122.932 215.710 1.00 59.36 ATOM 3515 CB PHE H 136 83.359 121.919 215.399 1.00 56.69 ATOM 3516 CG PHE H 136 84.659 122.545 214.976 1.00 62.32 ATOM 3517 CD1 PHE H 136 85.799 122.390 215.747 1.00 61.92 ATOM 3518 CE1 PHE H 136 86.995 122.958 215.364 1.00 56.95 ATOM 3519 CZ PHE H 136 87.067 123.698 214.194 1.00 60.87 ATOM 3520 CE2 PHE H 136 85.939 123.864 213.415 1.00 61.30 ATOM 3521 CD2 PHE H 136 84.741 123.288 213.808 1.00 65.69 ATOM 3522 C PHE H 136 81.009 122.193 216.194 1.00 59.03 ATOM 3523 O PHE H 136 80.928 121.812 217.358 1.00 55.79 ATOM 3524 N PRO H 137 80.039 121.980 215.296 1.00 59.70 ATOM 3525 CA PRO H 137 78.828 121.250 215.655 1.00 60.41 ATOM 3526 CB PRO H 137 77.959 121.376 214.396 1.00 61.25 ATOM 3527 CG PRO H 137 78.932 121.570 213.286 1.00 56.81 ATOM 3528 CD PRO H 137 80.027 122.408 213.885 1.00 62.15 ATOM 3529 C PRO H 137 79.089 119.773 215.946 1.00 60.80 ATOM 3530 O PRO H 137 79.987 119.164 215.359 1.00 57.22 ATOM 3531 N LEU H 138 78.304 119.222 216.865 1.00 60.53 ATOM 3532 CA LEU H 138 78.236 117.788 217.102 1.00 60.83 ATOM 3533 CB LEU H 138 78.461 117.478 218.585 1.00 60.60 ATOM 3534 CG LEU H 138 79.862 117.123 219.102 1.00 64.29 ATOM 3535 CD1 LEU H 138 80.967 117.378 218.081 1.00 60.02 ATOM 3536 CD2 LEU H 138 80.141 117.839 220.423 1.00 67.34 ATOM 3537 C LEU H 138 76.843 117.352 216.676 1.00 58.63 ATOM 3538 O LEU H 138 75.898 117.389 217.467 1.00 56.16 ATOM 3539 N ALA H 139 76.722 116.949 215.417 1.00 60.63 ATOM 3540 CA ALA H 139 75.425 116.706 214.795 1.00 61.11 ATOM 3541 CB ALA H 139 75.583 116.607 213.279 1.00 61.42 ATOM 3542 C ALA H 139 74.714 115.470 215.329 1.00 61.56 ATOM 3543 O ALA H 139 75.337 114.426 215.526 1.00 63.70 ATOM 3544 N PRO H 140 73.395 115.586 215.556 1.00 64.20 ATOM 3545 CA PRO H 140 72.571 114.437 215.909 1.00 62.68 ATOM 3546 CB PRO H 140 71.204 115.059 216.205 1.00 60.81 ATOM 3547 CG PRO H 140 71.196 116.331 215.446 1.00 65.26 ATOM 3548 CD PRO H 140 72.609 116.831 215.496 1.00 63.99 ATOM 3549 C PRO H 140 72.450 113.483 214.736 1.00 64.92 ATOM 3550 O PRO H 140 72.786 113.844 213.606 1.00 65.76 ATOM 3551 N SER H 141 71.965 112.277 215.009 1.00 67.65 ATOM 3552 CA SER H 141 71.770 111.263 213.982 1.00 68.48 ATOM 3553 CB SER H 141 73.087 110.969 213.258 1.00 68.44 ATOM 3554 OG SER H 141 74.087 110.524 214.159 1.00 64.01 ATOM 3555 C SER H 141 71.231 109.993 214.621 1.00 70.14 ATOM 3556 O SER H 141 70.705 110.028 215.732 1.00 69.04 ATOM 3557 N SER H 142 71.361 108.873 213.917 1.00 73.08 ATOM 3558 CA SER H 142 71.008 107.574 214.479 1.00 75.46 ATOM 3559 CB SER H 142 70.654 106.585 213.370 1.00 75.74 ATOM 3560 OG SER H 142 69.496 107.003 212.670 1.00 80.01 ATOM 3561 C SER H 142 72.165 107.041 215.320 1.00 76.21 ATOM 3562 O SER H 142 72.032 106.033 216.015 1.00 75.11 ATOM 3563 N LYS H 143 73.298 107.737 215.247 1.00 77.35 ATOM 3564 CA LYS H 143 74.499 167.376 215.993 1.00 78.88 ATOM 3565 CB LYS H 143 75.747 107.735 215.184 1.00 79.45 ATOM 3566 CG LYS H 143 75.825 107.034 213.834 1.00 84.49 ATOM 3567 CD LYS H 143 76.833 107.702 212.908 1.00 90.80 ATOM 3568 CE LYS H 143 76.401 109.114 212.540 1.00 89.61 ATOM 3569 NZ LYS H 143 77.225 109.683 211.439 1.00 90.31 ATOM 3570 C LYS H 143 74.525 108.077 217.351 1.00 78.76 ATOM 3571 O LYS H 143 75.314 107.729 218.234 1.00 75.78 ATOM 3572 N SER H 144 73.660 109.075 217.503 1.00 79.55 ATOM 3573 CA SER H 144 73.468 109.736 218.787 1.00 80.05 ATOM 3574 CB SER H 144 73.968 111.182 218.746 1.00 78.45 ATOM 3575 OG SER H 144 73.190 111.968 217.863 1.00 78.24 ATOM 3576 C SER H 144 71.997 109.681 219.197 1.00 81.06 ATOM 3577 O SER H 144 71.481 110.609 219.820 1.00 79.88 ATOM 3578 N THR H 145 71.334 108.580 218.842 1.00 82.54 ATOM 3579 CA THR H 145 69.929 108.361 219.187 1.00 83.46 ATOM 3580 CB THR H 145 69.079 108.055 217.928 1.00 83.46 ATOM 3581 OG1 THR H 145 68.829 109.271 217.212 1.00 79.59 ATOM 3582 CG2 THR H 145 67.745 107.417 218.303 1.00 82.60 ATOM 3583 C THR H 145 69.780 107.237 220.217 1.00 85.25 ATOM 3584 O THR H 145 70.419 106.192 220.104 1.00 85.12 ATOM 3585 N SER H 146 68.945 107.469 221.227 1.00 87.41 ATOM 3586 CA SER H 146 68.697 106.477 222.270 1.00 88.41 ATOM 3587 CB SER H 146 69.145 107.007 223.636 1.00 89.44 ATOM 3588 OG SER H 146 68.983 106.025 224.646 1.00 92.46 ATOM 3589 C SER H 146 67.220 106.088 222.312 1.00 87.43 ATOM 3590 O SER H 146 66.603 106.057 223.378 1.00 87.13 ATOM 3591 N GLY H 147 66.664 105.790 221.141 1.00 87.24 ATOM 3592 CA GLY H 147 65.254 105.430 221.021 1.00 83.78 ATOM 3593 C GLY H 147 64.389 106.629 220.678 1.00 80.59 ATOM 3594 O GLY H 147 64.210 106.964 219.505 1.00 80.08 ATOM 3595 N GLY H 148 63.851 107.275 221.706 1.00 75.67 ATOM 3596 CA GLY H 148 63.042 108.469 221.513 1.00 72.40 ATOM 3597 C GLY H 148 63.864 109.744 221.576 1.00 70.71 ATOM 3598 O GLY H 148 63.446 110.786 221.072 1.00 70.33 ATOM 3599 N THR H 149 65.041 109.663 222.190 1.00 66.12 ATOM 3600 CA THR H 149 65.871 110.845 222.398 1.00 66.33 ATOM 3601 CB THR H 149 66.124 111.100 223.899 1.00 66.76 ATOM 3602 OG1 THR H 149 66.835 109.990 224.460 1.00 70.47 ATOM 3603 CG2 THR H 149 64.800 111.272 224.636 1.00 66.35 ATOM 3604 C THR H 149 67.205 110.780 221.653 1.00 62.82 ATOM 3605 O THR H 149 67.752 109.702 221.428 1.00 61.46 ATOM 3606 N ALA H 150 67.714 111.948 221.273 1.00 59.37 ATOM 3607 CA ALA H 150 68.975 112.052 220.550 1.00 56.53 ATOM 3608 CB ALA H 150 68.732 112.550 219.138 1.00 55.17 ATOM 3609 C ALA H 150 69.925 112.990 221.278 1.00 56.69 ATOM 3610 O ALA H 150 69.503 113.776 222.122 1.00 55.86 ATOM 3611 N ALA H 151 71.208 112.906 220.945 1.00 55.41 ATOM 3612 CA ALA H 151 72.206 113.798 221.525 1.00 56.12 ATOM 3613 CB ALA H 151 73.320 112.999 222.192 1.00 52.67 ATOM 3614 C ALA H 151 72.780 114.720 220.459 1.00 57.64 ATOM 3615 O ALA H 151 72.945 114.329 219.306 1.00 60.82 ATOM 3616 N LEU H 152 73.069 115.951 220.848 1.00 59.35 ATOM 3617 CA LEU H 152 73.732 116.893 219.965 1.00 59.56 ATOM 3618 CB LEU H 152 72.708 117.650 219.122 1.00 60.73 ATOM 3619 CG LEU H 152 71.597 118.397 219.856 1.00 66.45 ATOM 3620 CD1 LEU H 152 72.028 119.820 220.129 1.00 71.75 ATOM 3621 CD2 LEU H 152 70.322 118.383 219.029 1.00 73.60 ATOM 3622 C LEU H 152 74.556 117.846 220.815 1.00 60.00 ATOM 3623 O LEU H 152 74.369 117.915 222.025 1.00 63.30 ATOM 3624 N GLY H 153 75.473 118.576 220.192 1.00 59.31 ATOM 3625 CA GLY H 153 76.325 119.466 220.950 1.00 58.94 ATOM 3626 C GLY H 153 77.259 120.327 220.133 1.00 62.41 ATOM 3627 O GLY H 153 77.096 120.484 218.921 1.00 62.78 ATOM 3628 N CYS H 154 78.243 120.887 220.823 1.00 63.67 ATOM 3629 CA CYS H 154 79.208 121.796 220.232 1.00 62.89 ATOM 3630 CB CYS H 154 78.828 123.248 220.535 1.00 67.73 ATOM 3631 SG CYS H 154 77.604 123.935 219.395 1.00 73.98 ATOM 3632 C CYS H 154 80.573 121.504 220.813 1.00 58.96 ATOM 3633 O CYS H 154 80.727 121.362 222.026 1.00 62.75 ATOM 3634 N LEU H 155 81.564 121.403 219.945 1.00 58.21 ATOM 3635 CA LEU H 155 82.935 121.234 220.383 1.00 56.76 ATOM 3636 CB LEU H 155 83.667 120.228 219.488 1.00 52.75 ATOM 3637 CG LEU H 155 85.180 120.078 219.684 1.00 56.76 ATOM 3638 CD1 LEU H 155 85.519 119.634 221.101 1.00 65.40 ATOM 3639 CD2 LEU H 155 85.762 119.112 218.672 1.00 52.13 ATOM 3640 C LEU H 155 83.614 122.594 220.345 1.00 52.36 ATOM 3641 O LEU H 155 83.707 123.222 219.289 1.00 55.47 ATOM 3642 N VAL H 156 84.059 123.057 221.509 1.00 58.71 ATOM 3643 CA VAL H 156 84.759 124.327 221.612 1.00 59.46 ATOM 3644 CB VAL H 156 84.273 125.118 222.829 1.00 60.79 ATOM 3645 CG1 VAL H 156 84.894 126.502 222.840 1.00 59.57 ATOM 3646 CG2 VAL H 156 82.750 125.207 222.818 1.00 57.69 ATOM 3647 C VAL H 156 86.255 124.052 221.730 1.00 59.80 ATOM 3648 O VAL H 156 86.753 123.687 222.800 1.00 59.62 ATOM 3649 N LYS H 157 86.971 124.227 220.626 1.00 57.32 ATOM 3650 CA LYS H 157 88.342 123.741 220.544 1.00 59.01 ATOM 3651 CB LYS H 157 88.498 122.802 219.346 1.00 54.06 ATOM 3652 CG LYS H 157 89.798 122.027 219.344 1.00 61.03 ATOM 3653 CD LYS H 157 89.778 120.909 218.320 1.00 58.83 ATOM 3654 CE LYS H 157 91.190 120.509 217.900 1.00 74.92 ATOM 3655 NZ LYS H 157 91.996 119.948 219.022 1.00 76.62 ATOM 3656 C LYS H 157 89.413 124.826 220.502 1.00 60.94 ATOM 3657 O LYS H 157 89.280 125.837 219.805 1.00 62.54 ATOM 3658 N ASP H 158 90.477 124.591 221.263 1.00 62.90 ATOM 3659 CA ASP H 158 91.712 125.363 221.157 1.00 63.81 ATOM 3660 CB ASP H 158 92.301 125.239 219.748 1.00 61.16 ATOM 3661 CG ASP H 158 92.803 123.832 219.445 1.00 70.75 ATOM 3662 OD1 ASP H 158 93.105 123.086 220.400 1.00 82.83 ATOM 3663 OD2 ASP H 158 92.896 123.467 218.255 1.00 72.24 ATOM 3664 C ASP H 158 91.540 126.825 221.559 1.00 63.84 ATOM 3665 O ASP H 158 91.656 127.728 220.731 1.00 67.25 ATOM 3666 N TYR H 159 91.267 127.052 222.838 1.00 63.07 ATOM 3667 CA TYR H 159 91.169 128.411 223.347 1.00 63.49 ATOM 3668 CB TYR H 159 89.722 128.764 223.698 1.00 61.67 ATOM 3669 CG TYR H 159 89.149 127.953 224.828 1.00 61.40 ATOM 3670 CD1 TYR H 159 88.564 126.714 224.592 1.00 59.32 ATOM 3671 CE1 TYR H 159 88.033 125.965 225.630 1.00 56.62 ATOM 3672 CZ TYR H 159 88.087 126.453 226.918 1.00 62.17 ATOM 3673 OH TYR H 159 87.565 125.716 227.952 1.00 61.18 ATOM 3674 CE2 TYR H 159 88.664 127.682 227.177 1.00 63.89 ATOM 3675 CD2 TYR H 159 89.189 128.424 226.135 1.00 60.46 ATOM 3676 C TYR H 159 92.071 128.601 224.552 1.00 61.14 ATOM 3677 O TYR H 159 92.477 127.634 225.196 1.00 61.97 ATOM 3678 N PHE H 160 92.381 129.858 224.847 1.00 61.15 ATOM 3679 CA PHE H 160 93.215 130.199 225.981 1.00 59.96 ATOM 3680 CB PHE H 160 94.687 129.925 225.664 1.00 59.46 ATOM 3681 CG PHE H 160 95.602 130.111 226.836 1.00 56.86 ATOM 3682 CD1 PHE H 160 95.953 129.035 227.631 1.00 52.82 ATOM 3683 CE1 PHE H 160 96.792 129.204 228.717 1.00 60.20 ATOM 3684 CZ PHE H 160 97.290 130.456 229.021 1.00 60.79 ATOM 3685 CE2 PHE H 160 96.948 131.540 228.238 1.00 57.69 ATOM 3686 CD2 PHE H 160 96.110 131.365 227.149 1.00 60.28 ATOM 3687 C PHE H 160 93.026 131.670 226.325 1.00 64.20 ATOM 3688 O PHE H 160 92.897 132.503 225.431 1.00 67.55 ATOM 3689 N PRO H 161 92.986 131.991 227.627 1.00 62.90 ATOM 3690 CA PRO H 161 92.904 131.021 228.711 1.00 62.53 ATOM 3691 CB PRO H 161 93.484 131.795 229.893 1.00 61.47 ATOM 3692 CG PRO H 161 93.037 133.200 229.638 1.00 65.16 ATOM 3693 CD PRO H 161 93.083 133.372 228.133 1.00 63.52 ATOM 3694 C PRO H 161 91.439 130.652 229.020 1.00 63.33 ATOM 3695 O PRO H 161 90.554 131.005 228.266 1.00 61.88 ATOM 3696 N GLU H 162 91.255 129.947 230.127 1.00 61.71 ATOM 3697 CA GLU H 162 89.922 129.735 230.665 1.00 63.14 ATOM 3698 CB GLU H 162 89.990 128.785 231.853 1.00 60.23 ATOM 3699 CG GLU H 162 90.208 127.335 231.484 1.00 68.72 ATOM 3700 CD GLU H 162 88.922 126.542 231.517 1.00 80.98 ATOM 3701 OE1 GLU H 162 87.967 126.915 230.798 1.00 86.87 ATOM 3702 OE2 GLU H 162 88.871 125.546 232.270 1.00 77.76 ATOM 3703 C GLU H 162 89.380 131.079 231.129 1.00 63.42 ATOM 3704 O GLU H 162 90.158 131.976 231.442 1.00 62.14 ATOM 3705 N PRO H 163 88.042 131.216 231.210 1.00 63.11 ATOM 3706 CA PRO H 163 87.029 130.236 230.861 1.00 61.95 ATOM 3707 CB PRO H 163 86.055 130.372 232.027 1.00 64.21 ATOM 3708 CG PRO H 163 86.122 131.866 232.384 1.00 59.99 ATOM 3709 CD PRO H 163 87.420 132.417 231.790 1.00 57.75 ATOM 3710 C PRO H 163 86.262 130.575 229.584 1.00 64.20 ATOM 3711 O PRO H 163 86.329 131.707 229.102 1.00 64.28 ATOM 3712 N VAL H 164 85.534 129.595 229.050 1.00 63.60 ATOM 3713 CA VAL H 164 84.421 129.886 228.155 1.00 63.95 ATOM 3714 CB VAL H 164 84.496 129.150 226.784 1.00 68.95 ATOM 3715 CG1 VAL H 164 85.891 129.226 226.179 1.00 64.74 ATOM 3716 CG2 VAL H 164 84.019 127.721 226.910 1.00 59.10 ATOM 3717 C VAL H 164 83.134 129.464 228.842 1.00 66.11 ATOM 3718 O VAL H 164 83.140 128.570 229.691 1.00 64.57 ATOM 3719 N THR H 165 82.035 130.119 228.477 1.00 66.49 ATOM 3720 CA THR H 165 80.709 129.690 228.896 1.00 65.82 ATOM 3721 CB THR H 165 79.939 130.828 229.587 1.00 67.55 ATOM 3722 OG1 THR H 165 79.920 131.977 228.730 1.00 71.77 ATOM 3723 CG2 THR H 165 80.603 131.193 230.894 1.00 67.74 ATOM 3724 C THR H 165 79.925 129.233 227.674 1.00 65.07 ATOM 3725 O THR H 165 80.191 129.677 226.562 1.00 63.74 ATOM 3726 N VAL H 166 78.964 128.340 227.878 1.00 67.69 ATOM 3727 CA VAL H 166 78.128 127.869 226.782 1.00 63.62 ATOM 3728 CB VAL H 166 78.555 126.463 226.290 1.00 65.73 ATOM 3729 CG1 VAL H 166 77.698 126.016 225.098 1.00 58.27 ATOM 3730 CG2 VAL H 166 80.032 126.443 225.926 1.00 58.18 ATOM 3731 C VAL H 166 76.677 127.817 227.228 1.00 66.64 ATOM 3732 O VAL H 166 76.358 127.228 228.263 1.00 68.24 ATOM 3733 N SER H 167 75.802 128.456 226.461 1.00 62.91 ATOM 3734 CA SER H 167 74.371 128.304 226.662 1.00 63.15 ATOM 3735 CB SER H 167 73.706 129.652 226.955 1.00 61.25 ATOM 3736 OG SER H 167 73.781 130.521 225.844 1.00 67.56 ATOM 3737 C SER H 167 73.774 127.659 225.419 1.00 62.55 ATOM 3738 O SER H 167 74.487 127.395 224.451 1.00 62.44 ATOM 3739 N TRP H 168 72.470 127.394 225.456 1.00 59.79 ATOM 3740 CA TRP H 168 71.766 126.808 224.319 1.00 53.14 ATOM 3741 CB TRP H 168 71.453 125.339 224.581 1.00 53.91 ATOM 3742 CG TRP H 168 72.633 124.436 224.414 1.00 51.93 ATOM 3743 CD1 TRP H 168 73.505 124.033 225.385 1.00 47.40 ATOM 3744 NE1 TRP H 168 74.461 123.203 224.846 1.00 55.69 ATOM 3745 CE2 TRP H 168 74.219 123.058 223.503 1.00 49.98 ATOM 3746 CD2 TRP H 168 73.076 123.825 223.195 1.00 55.31 ATOM 3747 CE3 TRP H 168 72.615 123.851 221.871 1.00 60.84 ATOM 3748 CZ3 TRP H 168 73.303 123.123 220.910 1.00 52.85 ATOM 3749 CH2 TRP H 168 74.435 122.365 221.251 1.00 53.43 ATOM 3750 CZ2 TRP H 168 74.907 122.322 222.539 1.00 50.25 ATOM 3751 C TRP H 168 70.481 127.560 224.042 1.00 54.62 ATOM 3752 O TRP H 168 69.732 127.879 224.961 1.00 59.59 ATOM 3753 N ASN H 169 70.229 127.831 222.766 1.00 57.68 ATOM 3754 CA ASN H 169 69.066 128.606 222.347 1.00 58.31 ATOM 3755 CB ASN H 169 67.793 127.760 222.403 1.00 57.06 ATOM 3756 CG ASN H 169 67.801 126.635 221.395 1.00 58.24 ATOM 3757 OD1 ASN H 169 66.928 125.768 221.408 1.00 65.71 ATOM 3758 ND2 ASN H 169 68.787 126.644 220.507 1.00 59.76 ATOM 3759 C ASN H 169 68.899 129.879 223.163 1.00 58.49 ATOM 3760 O ASN H 169 67.780 130.307 223.442 1.00 55.71 ATOM 3761 N SER H 170 70.025 130.475 223.542 1.00 57.78 ATOM 3762 CA SER H 170 70.029 131.740 224.267 1.00 59.83 ATOM 3763 CB SER H 170 69.244 132.804 223.497 1.00 56.49 ATOM 3764 OG SER H 170 69.876 133.091 222.263 1.00 57.17 ATOM 3765 C SER H 170 69.474 131.595 225.675 1.00 60.31 ATOM 3766 O SER H 170 68.932 132.545 226.235 1.00 61.80 ATOM 3767 N GLY H 171 69.615 130.405 226.245 1.00 59.95 ATOM 3768 CA GLY H 171 69.104 130.139 227.582 1.00 61.64 ATOM 3769 C GLY H 171 67.777 129.402 227.593 1.00 61.13 ATOM 3770 O GLY H 171 67.356 128.901 228.630 1.00 65.78 ATOM 3771 N ALA H 172 67.115 129.321 226.443 1.00 60.20 ATOM 3772 CA ALA H 172 65.806 128.671 226.375 1.00 60.64 ATOM 3773 CB ALA H 172 65.126 128.968 225.045 1.00 60.47 ATOM 3774 C ALA H 172 65.886 127.163 226.613 1.00 60.70 ATOM 3775 O ALA H 172 64.891 126.530 226.957 1.00 61.62 ATOM 3776 N LEU H 173 67.075 126.594 226.431 1.00 61.51 ATOM 3777 CA LEU H 173 67.291 125.169 226.632 1.00 57.56 ATOM 3778 CB LEU H 173 67.832 124.542 225.350 1.00 59.84 ATOM 3779 CG LEU H 173 67.465 123.112 224.948 1.00 60.94 ATOM 3780 CD1 LEU H 173 68.435 122.646 223.875 1.00 64.14 ATOM 3781 CD2 LEU H 173 67.460 122.147 226.115 1.00 62.21 ATOM 3782 C LEU H 173 68.314 124.992 227.739 1.00 60.03 ATOM 3783 O LEU H 173 69.470 125.386 227.575 1.00 59.49 ATOM 3784 N THR H 174 67.888 124.405 228.860 1.00 56.18 ATOM 3785 CA THR H 174 68.771 124.161 229.999 1.00 55.33 ATOM 3786 CB THR H 174 68.398 125.050 231.204 1.00 56.03 ATOM 3787 OG1 THR H 174 67.046 124.777 231.597 1.00 56.80 ATOM 3788 CG2 THR H 174 68.525 126.527 230.844 1.00 57.53 ATOM 3789 C THR H 174 68.733 122.703 230.459 1.00 57.42 ATOM 3790 O THR H 174 69.734 122.163 230.926 1.00 58.14 ATOM 3791 N SER H 175 67.571 122.071 230.345 1.00 55.98 ATOM 3792 CA SER H 175 67.418 120.690 230.787 1.00 58.33 ATOM 3793 CB SER H 175 65.940 120.305 230.837 1.00 59.84 ATOM 3794 OG SER H 175 65.221 121.167 231.698 1.00 61.92 ATOM 3795 C SER H 175 68.170 119.756 229.853 1.00 55.33 ATOM 3796 O SER H 175 68.197 119.976 228.651 1.00 56.65 ATOM 3797 N GLY H 176 68.803 118.733 230.415 1.00 59.28 ATOM 3798 CA GLY H 176 69.528 117.748 229.622 1.00 60.80 ATOM 3799 C GLY H 176 70.894 118.214 229.152 1.00 61.34 ATOM 3800 O GLY H 176 71.617 117.470 228.497 1.00 62.23 ATOM 3801 N VAL H 177 71.258 119.445 229.486 1.00 62.68 ATOM 3802 CA VAL H 177 72.538 119.988 229.052 1.00 57.97 ATOM 3803 CB VAL H 177 72.510 121.525 229.017 1.00 61.00 ATOM 3804 CG1 VAL H 177 73.895 122.085 228.676 1.00 55.61 ATOM 3805 CG2 VAL H 177 71.463 122.007 228.021 1.00 57.09 ATOM 3806 C VAL H 177 73.678 119.523 229.951 1.00 61.10 ATOM 3807 O VAL H 177 73.556 119.525 231.180 1.00 62.04 ATOM 3808 N HIS H 178 74.773 119.095 229.330 1.00 59.06 ATOM 3809 CA HIS H 178 76.020 118.861 230.048 1.00 59.55 ATOM 3810 CB HIS H 178 76.365 117.371 230.093 1.00 53.27 ATOM 3811 CG HIS H 178 75.491 116.573 231.005 1.00 56.56 ATOM 3812 ND1 HIS H 178 74.652 115.579 230.550 1.00 64.16 ATOM 3813 CE1 HIS H 178 74.003 115.049 231.572 1.00 58.54 ATOM 3814 NE2 HIS H 178 74.393 115.662 232.676 1.00 61.60 ATOM 3815 CD2 HIS H 178 75.320 116.624 232.349 1.00 57.83 ATOM 3816 C HIS H 178 77.149 119.626 229.370 1.00 59.65 ATOM 3817 O HIS H 178 77.501 119.332 228.232 1.00 62.69 ATOM 3818 N THR H 179 77.706 120.613 230.064 1.00 58.82 ATOM 3819 CA THR H 179 78.887 121.324 229.575 1.00 60.66 ATOM 3820 CB THR H 179 78.735 122.856 229.729 1.00 60.58 ATOM 3821 OG1 THR H 179 77.541 123.290 229.065 1.00 61.88 ATOM 3822 CG2 THR H 179 79.933 123.589 229.136 1.00 51.76 ATOM 3823 C THR H 179 80.085 120.839 230.384 1.00 62.67 ATOM 3824 O THR H 179 80.151 121.064 231.593 1.00 66.55 ATOM 3825 N PHE H 180 81.024 120.170 229.723 1.00 56.86 ATOM 3826 CA PHE H 180 82.109 119.490 230.428 1.00 56.67 ATOM 3827 CB PHE H 180 82.694 118.373 229.557 1.00 52.97 ATOM 3828 CG PHE H 180 81.744 117.245 229.312 1.00 55.62 ATOM 3829 CD1 PHE H 180 80.788 117.331 228.311 1.00 55.46 ATOM 3830 CE1 PHE H 180 79.902 116.293 228.089 1.00 56.83 ATOM 3831 CZ PHE H 180 79.967 115.157 228.869 1.00 58.05 ATOM 3832 CE2 PHE H 180 80.921 115.061 229.870 1.00 55.14 ATOM 3833 CD2 PHE H 180 81.799 116.099 230.087 1.00 54.75 ATOM 3834 C PHE H 180 83.222 120.435 230.848 1.00 55.77 ATOM 3835 O PHE H 180 83.487 121.427 230.169 1.00 55.59 ATOM 3836 N PRO H 181 83.901 120.118 231.962 1.00 55.07 ATOM 3837 CA PRO H 181 85.076 120.914 232.326 1.00 57.90 ATOM 3838 CB PRO H 181 85.633 120.191 233.556 1.00 48.83 ATOM 3839 CG PRO H 181 84.469 119.417 234.106 1.00 57.74 ATOM 3840 CD PRO H 181 83.626 119.041 232.929 1.00 57.06 ATOM 3841 C PRO H 181 86.097 120.905 231.190 1.00 57.37 ATOM 3842 O PRO H 181 86.177 119.938 230.437 1.00 61.54 ATOM 3843 N ALA H 182 86.862 121.978 231.058 1.00 60.43 ATOM 3844 CA ALA H 182 87.846 122.067 229.989 1.00 58.14 ATOM 3845 CB ALA H 182 88.443 123.456 229.930 1.00 60.11 ATOM 3846 C ALA H 182 88.941 121.038 230.172 1.00 61.69 ATOM 3847 O ALA H 182 89.242 120.619 231.290 1.00 62.77 ATOM 3848 N VAL H 183 89.535 120.626 229.061 1.00 61.58 ATOM 3849 CA VAL H 183 90.699 119.767 229.109 1.00 64.83 ATOM 3850 CB VAL H 183 90.479 118.487 228.285 1.00 61.62 ATOM 3851 CG1 VAL H 183 91.768 117.713 228.164 1.00 69.82 ATOM 3852 CG2 VAL H 183 89.407 117.627 228.936 1.00 69.94 ATOM 3853 C VAL H 183 91.885 120.555 228.571 1.00 63.05 ATOM 3854 O VAL H 183 91.758 121.264 227.576 1.00 66.28 ATOM 3855 N LEU H 184 93.027 120.461 229.243 1.00 63.86 ATOM 3856 CA LEU H 184 94.228 121.124 228.760 1.00 64.07 ATOM 3857 CB LEU H 184 95.144 121.526 229.917 1.00 64.08 ATOM 3858 CG LEU H 184 96.424 122.257 229.499 1.00 62.76 ATOM 3859 CD1 LEU H 184 96.090 123.544 228.775 1.00 61.31 ATOM 3860 CD2 LEU H 184 97.312 122.540 230.698 1.00 65.03 ATOM 3861 C LEU H 184 94.965 120.201 227.807 1.00 65.98 ATOM 3862 O LEU H 184 95.547 119.202 228.226 1.00 68.01 ATOM 3863 N GLN H 185 94.938 120.541 226.523 1.00 67.54 ATOM 3864 CA GLN H 185 95.613 119.741 225.510 1.00 69.24 ATOM 3865 CB GLN H 185 95.160 120.166 224.112 1.00 69.69 ATOM 3866 CG GLN H 185 93.666 119.954 223.882 1.00 73.83 ATOM 3867 CD GLN H 185 93.108 120.798 222.754 1.00 74.88 ATOM 3868 OE1 GLN H 185 92.404 120.294 221.881 1.00 79.17 ATOM 3869 NE2 GLN H 185 93.412 122.091 222.770 1.00 67.34 ATOM 3870 C GLN H 185 97.124 119.860 225.652 1.00 70.14 ATOM 3871 O GLN H 185 97.624 120.740 226.356 1.00 69.07 ATOM 3872 N SER H 186 97.850 118.961 224.995 1.00 72.93 ATOM 3873 CA SER H 186 99.306 118.991 225.030 1.00 75.55 ATOM 3874 CB SER H 186 99.891 117.746 224.360 1.00 76.56 ATOM 3875 OG SER H 186 99.329 117.552 223.075 1.00 84.08 ATOM 3876 C SER H 186 99.840 120.261 224.370 1.00 75.13 ATOM 3877 O SER H 186 100.913 120.752 224.726 1.00 77.40 ATOM 3878 N SER H 187 99.076 120.793 223.419 1.00 72.79 ATOM 3879 CA SER H 187 99.435 122.032 222.731 1.00 68.76 ATOM 3880 CB SER H 187 98.507 122.267 221.531 1.00 67.10 ATOM 3881 OG SER H 187 97.143 122.307 221.928 1.00 67.06 ATOM 3882 C SER H 187 99.416 123.242 223.674 1.00 67.58 ATOM 3883 O SER H 187 99.937 124.305 223.344 1.00 64.36 ATOM 3884 N GLY H 188 98.818 123.070 224.850 1.00 66.92 ATOM 3885 CA GLY H 188 98.747 124.144 225.838 1.00 64.84 ATOM 3886 C GLY H 188 97.444 124.917 225.767 1.00 64.56 ATOM 3887 O GLY H 188 97.208 125.831 226.557 1.00 65.58 ATOM 3888 N LEU H 189 96.593 124.544 224.816 1.00 63.38 ATOM 3889 CA LEU H 189 95.306 125.198 224.631 1.00 60.94 ATOM 3890 CB LEU H 189 95.039 125.448 223.146 1.00 58.53 ATOM 3891 CG LEU H 189 96.051 126.327 222.404 1.00 61.66 ATOM 3892 CD1 LEU H 189 95.825 126.240 220.905 1.00 49.85 ATOM 3893 CD2 LEU H 189 95.982 127.781 222.881 1.00 57.27 ATOM 3894 C LEU H 189 94.198 124.342 225.221 1.00 61.40 ATOM 3895 O LEU H 189 94.348 123.130 225.352 1.00 63.33 ATOM 3896 N TYR H 190 93.084 124.977 225.572 1.00 61.40 ATOM 3897 CA TYR H 190 91.962 124.270 226.183 1.00 64.61 ATOM 3898 CB TYR H 190 91.282 125.146 227.239 1.00 62.75 ATOM 3899 CG TYR H 190 92.123 125.422 228.463 1.00 62.48 ATOM 3900 CD1 TYR H 190 92.056 124.591 229.579 1.00 58.38 ATOM 3901 CE1 TYR H 190 92.823 124.845 230.706 1.00 58.75 ATOM 3902 CZ TYR H 190 93.666 125.943 230.724 1.00 59.27 ATOM 3903 OH TYR H 190 94.429 126.205 231.842 1.00 62.63 ATOM 3904 CE2 TYR H 190 93.747 126.782 229.629 1.00 58.07 ATOM 3905 CD2 TYR H 190 92.977 126.520 228.509 1.00 56.96 ATOM 3906 C TYR H 190 90.924 123.828 225.160 1.00 63.15 ATOM 3907 O TYR H 190 90.819 124.396 224.073 1.00 64.54 ATOM 3908 N SER H 191 90.160 122.808 225.525 1.00 60.90 ATOM 3909 CA SER H 191 89.014 122.380 224.740 1.00 61.15 ATOM 3910 CB SER H 191 89.397 121.274 223.751 1.00 59.23 ATOM 3911 OG SER H 191 90.257 121.763 222.739 1.00 61.94 ATOM 3912 C SER H 191 87.954 121.850 225.681 1.00 60.33 ATOM 3913 O SER H 191 88.269 121.224 226.688 1.00 59.58 ATOM 3914 N LEU H 192 86.697 122.107 225.349 1.00 60.06 ATOM 3915 CA LEU H 192 85.593 121.472 226.046 1.00 65.31 ATOM 3916 CB LEU H 192 85.058 122.362 227.178 1.00 61.76 ATOM 3917 CG LEU H 192 84.375 123.698 226.869 1.00 66.61 ATOM 3918 CD1 LEU H 192 82.989 123.488 226.274 1.00 58.27 ATOM 3919 CD2 LEU H 192 84.278 124.538 228.143 1.00 65.42 ATOM 3920 C LEU H 192 84.497 121.143 225.053 1.00 65.10 ATOM 3921 O LEU H 192 84.506 121.625 223.921 1.00 69.10 ATOM 3922 N SER H 193 83.560 120.310 225.479 1.00 66.02 ATOM 3923 CA SER H 193 82.372 120.050 224.693 1.00 66.30 ATOM 3924 CB SER H 193 82.330 118.588 224.259 1.00 67.58 ATOM 3925 OG SER H 193 82.571 117.728 225.362 1.00 80.05 ATOM 3926 C SER H 193 81.152 120.391 225.534 1.00 63.98 ATOM 3927 O SER H 193 81.208 120.360 226.759 1.00 65.64 ATOM 3928 N SER H 194 80.063 120.753 224.870 1.00 61.97 ATOM 3929 CA SER H 194 78.782 120.890 225.535 1.00 58.26 ATOM 3930 CB SER H 194 78.325 122.341 225.561 1.00 57.58 ATOM 3931 OG SER H 194 77.101 122.455 226.268 1.00 64.75 ATOM 3932 C SER H 194 77.791 120.063 224.751 1.00 61.19 ATOM 3933 O SER H 194 77.734 120.159 223.526 1.00 58.55 ATOM 3934 N VAL H 195 77.018 119.238 225.446 1.00 59.04 ATOM 3935 CA VAL H 195 76.041 118.399 224.767 1.00 60.25 ATOM 3936 CB VAL H 195 76.451 116.910 224.753 1.00 59.77 ATOM 3937 CG1 VAL H 195 77.876 116.738 224.211 1.00 58.12 ATOM 3938 CG2 VAL H 195 76.313 116.303 226.143 1.00 53.19 ATOM 3939 C VAL H 195 74.679 118.532 225.421 1.00 61.73 ATOM 3940 O VAL H 195 74.564 118.973 226.564 1.00 62.28 ATOM 3941 N VAL H 196 73.649 118.145 224.686 1.00 59.99 ATOM 3942 CA VAL H 196 72.299 118.164 225.205 1.00 61.17 ATOM 3943 CB VAL H 196 71.593 119.517 224.915 1.00 58.47 ATOM 3944 CG1 VAL H 196 71.459 119.742 223.435 1.00 60.94 ATOM 3945 CG2 VAL H 196 70.219 119.567 225.576 1.00 61.81 ATOM 3946 C VAL H 196 71.538 117.012 224.568 1.00 62.15 ATOM 3947 O VAL H 196 71.717 116.711 223.387 1.00 61.55 ATOM 3948 N THR H 197 70.710 116.344 225.358 1.00 61.31 ATOM 3949 CA THR H 197 69.868 115.297 224.823 1.00 59.11 ATOM 3950 CB THR H 197 69.867 114.051 225.720 1.00 60.80 ATOM 3951 OG1 THR H 197 69.493 114.417 227.051 1.00 66.87 ATOM 3952 CG2 THR H 197 71.257 113.431 225.749 1.00 56.53 ATOM 3953 C THR H 197 68.461 115.841 224.609 1.00 60.99 ATOM 3954 O THR H 197 67.910 116.536 225.465 1.00 60.63 ATOM 3955 N VAL H 198 67.897 115.541 223.445 1.00 59.68 ATOM 3956 CA VAL H 198 66.602 116.074 223.054 1.00 61.72 ATOM 3957 CB VAL H 198 66.763 117.242 222.051 1.00 62.30 ATOM 3958 CG1 VAL H 198 67.667 118.316 222.625 1.00 62.96 ATOM 3959 CG2 VAL H 198 67.318 116.738 220.731 1.00 59.08 ATOM 3960 C VAL H 198 65.777 114.965 222.413 1.00 62.94 ATOM 3961 O VAL H 198 66.328 113.937 222.022 1.00 65.04 ATOM 3962 N PRO H 199 64.452 115.157 222.311 1.00 63.42 ATOM 3963 CA PRO H 199 63.622 114.168 221.623 1.00 61.90 ATOM 3964 CB PRO H 199 62.201 114.723 221.781 1.00 59.09 ATOM 3965 CG PRO H 199 62.278 115.696 222.904 1.00 63.60 ATOM 3966 CD PRO H 199 63.654 116.276 222.838 1.00 64.72 ATOM 3967 C PRO H 199 63.982 114.074 220.142 1.00 62.36 ATOM 3968 O PRO H 199 64.045 115.094 219.454 1.00 63.75 ATOM 3969 N SER H 200 64.218 112.860 219.658 1.00 62.46 ATOM 3970 CA SER H 200 64.551 112.653 218.253 1.00 63.98 ATOM 3971 CB SER H 200 64.830 111.175 217.980 1.00 63.13 ATOM 3972 OG SER H 200 63.666 110.391 218.172 1.00 64.81 ATOM 3973 C SER H 200 63.440 113.160 217.334 1.00 64.98 ATOM 3974 O SER H 200 63.673 113.434 216.157 1.00 67.17 ATOM 3975 N SER H 201 62.237 113.292 217.884 1.00 66.98 ATOM 3976 CA SER H 201 61.066 113.719 217.119 1.00 67.87 ATOM 3977 CB SER H 201 59.784 113.377 217.886 1.00 68.04 ATOM 3978 OG SER H 201 59.857 113.835 219.229 1.00 72.22 ATOM 3979 C SER H 201 61.083 115.209 216.773 1.00 67.40 ATOM 3980 O SER H 201 60.332 115.658 215.907 1.00 68.03 ATOM 3981 N SER H 202 61.941 115.969 217.446 1.00 67.07 ATOM 3982 CA SER H 202 61.998 117.414 217.249 1.00 66.11 ATOM 3983 CB SER H 202 61.949 118.134 218.598 1.00 67.53 ATOM 3984 OG SER H 202 63.199 118.048 219.264 1.00 67.16 ATOM 3985 C SER H 202 63.244 117.849 216.479 1.00 65.78 ATOM 3986 O SER H 202 63.526 119.040 216.366 1.00 65.89 ATOM 3987 N LEU H 203 63.990 116.884 215.953 1.00 65.30 ATOM 3988 CA LEU H 203 65.203 117.184 215.199 1.00 66.00 ATOM 3989 CB LEU H 203 66.026 115.913 214.973 1.00 66.64 ATOM 3990 CG LEU H 203 66.658 115.253 216.199 1.00 63.72 ATOM 3991 CD1 LEU H 203 67.345 113.953 215.806 1.00 62.23 ATOM 3992 CD2 LEU H 203 67.639 116.202 216.865 1.00 65.60 ATOM 3993 C LEU H 203 64.891 117.847 213.858 1.00 68.40 ATOM 3994 O LEU H 203 65.777 118.409 213.212 1.00 68.93 ATOM 3995 N GLY H 204 63.629 117.775 213.443 1.00 68.74 ATOM 3996 CA GLY H 204 63.195 118.388 212.195 1.00 71.19 ATOM 3997 C GLY H 204 62.369 119.646 212.395 1.00 73.16 ATOM 3998 O GLY H 204 62.248 120.465 211.486 1.00 74.56 ATOM 3999 N THR H 205 61.802 119.802 213.588 1.00 74.64 ATOM 4000 CA THR H 205 60.942 120.947 213.885 1.00 76.03 ATOM 4001 CB THR H 205 59.598 120.501 214.502 1.00 76.65 ATOM 4002 OG1 THR H 205 59.833 119.885 215.774 1.00 79.50 ATOM 4003 CG2 THR H 205 58.892 119.514 213.589 1.00 74.82 ATOM 4004 C THR H 205 61.605 121.960 214.820 1.00 75.88 ATOM 4005 O THR H 205 61.180 123.113 214.899 1.00 76.17 ATOM 4006 N GLN H 206 62.647 121.528 215.523 1.00 74.79 ATOM 4007 CA GLN H 206 63.322 122.390 216.488 1.00 73.37 ATOM 4008 CB GLN H 206 63.335 121.741 217.874 1.00 74.10 ATOM 4009 CG GLN H 206 62.293 122.305 218.823 1.00 77.23 ATOM 4010 CD GLN H 206 62.609 123.731 219.240 1.00 75.83 ATOM 4011 OE1 GLN H 206 63.768 124.077 219.477 1.00 64.12 ATOM 4012 NE2 GLN H 206 61.578 124.566 219.330 1.00 68.55 ATOM 4013 C GLN H 206 64.738 122.774 216.075 1.00 71.97 ATOM 4014 O GLN H 206 65.547 121.923 215.701 1.00 72.88 ATOM 4015 N THR H 207 65.025 124.070 216.146 1.00 67.63 ATOM 4016 CA THR H 207 66.359 124.581 215.878 1.00 65.76 ATOM 4017 CB THR H 207 66.313 126.007 215.293 1.00 65.17 ATOM 4018 OG1 THR H 207 65.682 125.982 214.005 1.00 67.23 ATOM 4019 CG2 THR H 207 67.713 126.567 215.149 1.00 60.94 ATOM 4020 C THR H 207 67.183 124.588 217.163 1.00 64.68 ATOM 4021 O THR H 207 66.699 124.986 218.223 1.00 65.67 ATOM 4022 N TYR H 208 68.427 124.135 217.063 1.00 62.84 ATOM 4023 CA TYR H 208 69.325 124.102 218.204 1.00 60.30 ATOM 4024 CB TYR H 208 69.666 122.659 218.573 1.00 60.65 ATOM 4025 CG TYR H 208 68.469 121.872 219.043 1.00 59.93 ATOM 4026 CD1 TYR H 208 67.971 122.044 220.324 1.00 56.46 ATOM 4027 CE1 TYR H 208 66.868 121.335 220.767 1.00 60.75 ATOM 4028 CZ TYR H 208 66.246 120.439 219.926 1.00 59.33 ATOM 4029 OH TYR H 208 65.152 119.743 220.386 1.00 63.41 ATOM 4030 CE2 TYR H 208 66.717 120.247 218.638 1.00 57.55 ATOM 4031 CD2 TYR H 208 67.824 120.967 218.202 1.00 55.88 ATOM 4032 C TYR H 208 70.587 124.897 217.910 1.00 62.11 ATOM 4033 O TYR H 208 71.263 124.659 216.909 1.00 64.87 ATOM 4034 N ILE H 209 70.886 125.850 218.785 1.00 61.03 ATOM 4035 CA ILE H 209 72.028 126.737 218.617 1.00 60.95 ATOM 4036 CB ILE H 209 71.581 128.167 218.221 1.00 59.96 ATOM 4037 CG1 ILE H 209 70.717 128.136 216.960 1.00 61.47 ATOM 4038 CD1 ILE H 209 70.265 129.503 216.491 1.00 64.77 ATOM 4039 CG2 ILE H 209 72.785 129.077 218.027 1.00 56.13 ATOM 4040 C ILE H 209 72.786 126.821 219.931 1.00 60.12 ATOM 4041 O ILE H 209 72.200 127.117 220.967 1.00 65.73 ATOM 4042 N CYS H 210 74.083 126.546 219.900 1.00 61.35 ATOM 4043 CA CYS H 210 74.902 126.738 221.085 1.00 63.03 ATOM 4044 CB CYS H 210 75.947 125.639 221.217 1.00 65.22 ATOM 4045 SG CYS H 210 77.306 125.823 220.077 1.00 70.31 ATOM 4046 C CYS H 210 75.575 128.107 221.032 1.00 62.72 ATOM 4047 O CYS H 210 76.136 128.507 220.009 1.00 62.35 ATOM 4048 N ASN H 211 75.498 128.826 222.143 1.00 59.46 ATOM 4049 CA ASN H 211 76.048 130.164 222.232 1.00 60.98 ATOM 4050 CB ASN H 211 75.033 131.108 222.878 1.00 57.29 ATOM 4051 CG ASN H 211 73.608 130.845 222.407 1.00 62.97 ATOM 4052 OD1 ASN H 211 73.252 131.131 221.262 1.00 62.84 ATOM 4053 ND2 ASN H 211 72.787 130.293 223.294 1.00 54.56 ATOM 4054 C ASN H 211 77.325 130.120 223.048 1.00 62.06 ATOM 4055 O ASN H 211 77.293 129.867 224.254 1.00 65.41 ATOM 4056 N VAL H 212 78.452 130.353 222.389 1.00 62.66 ATOM 4057 CA VAL H 212 79.742 130.267 223.060 1.00 64.80 ATOM 4058 CB VAL H 212 80.744 129.422 222.256 1.00 64.65 ATOM 4059 CG1 VAL H 212 82.085 129.346 222.995 1.00 58.00 ATOM 4060 CG2 VAL H 212 80.175 128.024 222.003 1.00 58.60 ATOM 4061 C VAL H 212 80.335 131.644 223.299 1.00 65.38 ATOM 4062 O VAL H 212 80.471 132.440 222.371 1.00 69.31 ATOM 4063 N ASN H 213 80.692 131.920 224.548 1.00 64.88 ATOM 4064 CA ASN H 213 81.340 133.184 224.887 1.00 67.52 ATOM 4065 CB ASN H 213 80.446 134.034 225.798 1.00 64.90 ATOM 4066 CG ASN H 213 80.861 135.499 225.824 1.00 81.17 ATOM 4067 OD1 ASN H 213 81.715 135.932 225.046 1.00 89.05 ATOM 4068 ND2 ASN H 213 80.257 136.269 226.722 1.00 86.87 ATOM 4069 C ASN H 213 82.714 132.961 225.523 1.00 65.38 ATOM 4070 O ASN H 213 82.857 132.191 226.477 1.00 65.84 ATOM 4071 N HIS H 214 83.725 133.618 224.964 1.00 61.97 ATOM 4072 CA HIS H 214 85.075 133.561 225.513 1.00 62.56 ATOM 4073 CB HIS H 214 86.005 132.775 224.594 1.00 60.95 ATOM 4074 CG HIS H 214 87.391 132.608 225.131 1.00 60.21 ATOM 4075 ND1 HIS H 214 88.493 133.177 224.533 1.00 60.25 ATOM 4076 CE1 HIS H 214 89.578 132.858 225.217 1.00 59.58 ATOM 4077 NE2 HIS H 214 89.216 132.106 226.242 1.00 62.96 ATOM 4078 CD2 HIS H 214 87.855 131.931 226.209 1.00 55.38 ATOM 4079 C HIS H 214 85.586 134.984 225.712 1.00 64.11 ATOM 4080 O HIS H 214 86.203 135.572 224.816 1.00 60.97 ATOM 4081 N LYS H 215 85.321 135.529 226.897 1.00 59.93 ATOM 4082 CA LYS H 215 85.648 136.918 227.198 1.00 59.23 ATOM 4083 CB LYS H 215 85.256 137.273 228.630 1.00 59.77 ATOM 4084 CG LYS H 215 83.777 137.153 228.920 1.00 66.44 ATOM 4085 CD LYS H 215 83.443 137.807 230.254 1.00 86.69 ATOM 4086 CE LYS H 215 82.069 137.384 230.758 1.00 98.10 ATOM 4087 NZ LYS H 215 80.987 137.732 229.798 1.00 106.28 ATOM 4088 C LYS H 215 87.107 137.277 226.961 1.00 57.38 ATOM 4089 O LYS H 215 87.387 138.316 226.358 1.00 60.96 ATOM 4090 N PRO H 216 88.047 136.432 227.438 1.00 59.30 ATOM 4091 CA PRO H 216 89.464 136.777 227.290 1.00 59.52 ATOM 4092 CB PRO H 216 90.182 135.508 227.755 1.00 55.80 ATOM 4093 CG PRO H 216 89.217 134.906 228.755 1.00 56.74 ATOM 4094 CD PRO H 216 87.872 135.147 228.145 1.00 58.17 ATOM 4095 C PRO H 216 89.868 137.152 225.863 1.00 61.61 ATOM 4096 O PRO H 216 90.794 137.938 225.683 1.00 65.14 ATOM 4097 N SER H 217 89.175 136.613 224.863 1.00 60.26 ATOM 4098 CA SER H 217 89.465 136.957 223.470 1.00 61.16 ATOM 4099 CB SER H 217 89.703 135.696 222.646 1.00 61.45 ATOM 4100 OG SER H 217 88.550 134.875 222.655 1.00 54.33 ATOM 4101 C SER H 217 88.348 137.769 222.826 1.00 60.53 ATOM 4102 O SER H 217 88.371 138.013 221.624 1.00 59.11 ATOM 4103 N ASN H 218 87.371 138.176 223.629 1.00 64.04 ATOM 4104 CA ASN H 218 86.191 138.882 223.126 1.00 65.09 ATOM 4105 CB ASN H 218 86.572 140.269 222.613 1.00 63.75 ATOM 4106 CG ASN H 218 87.271 141.108 223.666 1.00 70.69 ATOM 4107 OD1 ASN H 218 88.437 141.476 223.507 1.00 72.99 ATOM 4108 ND2 ASN H 218 86.563 141.416 224.751 1.00 55.26 ATOM 4109 C ASN H 218 85.444 138.105 222.037 1.00 65.03 ATOM 4110 O ASN H 218 84.762 138.698 221.204 1.00 66.32 ATOM 4111 N THR H 219 85.576 136.781 222.053 1.00 64.62 ATOM 4112 CA THR H 219 84.927 135.920 221.066 1.00 65.89 ATOM 4113 CB THR H 219 85.747 134.632 220.833 1.00 67.75 ATOM 4114 OG1 THR H 219 87.080 134.979 220.431 1.00 73.65 ATOM 4115 CG2 THR H 219 85.105 133.767 219.752 1.00 63.66 ATOM 4116 C THR H 219 83.499 135.535 221.469 1.00 66.64 ATOM 4117 O THR H 219 83.273 135.001 222.554 1.00 67.32 ATOM 4118 N LYS H 220 82.539 135.828 220.596 1.00 67.71 ATOM 4119 CA LYS H 220 81.168 135.344 220.755 1.00 69.25 ATOM 4120 CB LYS H 220 80.194 136.498 220.995 1.00 70.79 ATOM 4121 CG LYS H 220 80.254 137.104 222.382 1.00 75.54 ATOM 4122 CD LYS H 220 79.036 137.976 222.651 1.00 93.01 ATOM 4123 CE LYS H 220 79.016 138.465 224.093 1.00 100.56 ATOM 4124 NZ LYS H 220 77.747 139.173 224.426 1.00 103.95 ATOM 4125 C LYS H 220 80.756 134.587 219.499 1.00 69.44 ATOM 4126 O LYS H 220 80.845 135.117 218.391 1.00 67.36 ATOM 4127 N VAL H 221 80.314 133.347 219.671 1.00 68.83 ATOM 4128 CA VAL H 221 79.932 132.511 218.536 1.00 66.91 ATOM 4129 CB VAL H 221 81.023 131.457 218.217 1.00 66.95 ATOM 4130 CG1 VAL H 221 80.566 130.523 217.104 1.00 71.51 ATOM 4131 CG2 VAL H 221 82.329 132.135 217.827 1.00 69.00 ATOM 4132 C VAL H 221 78.607 131.796 218.795 1.00 64.39 ATOM 4133 O VAL H 221 78.432 131.160 219.830 1.00 68.73 ATOM 4134 N ASP H 222 77.672 131.921 217.860 1.00 61.13 ATOM 4135 CA ASP H 222 76.451 131.127 217.892 1.00 60.01 ATOM 4136 CB ASP H 222 75.216 132.010 217.722 1.00 60.32 ATOM 4137 CG ASP H 222 75.135 133.104 218.768 1.00 65.14 ATOM 4138 OD1 ASP H 222 75.064 132.785 219.976 1.00 67.99 ATOM 4139 OD2 ASP H 222 75.144 134.288 218.380 1.00 62.58 ATOM 4140 C ASP H 222 76.527 130.112 216.766 1.00 61.37 ATOM 4141 O ASP H 222 76.556 130.481 215.591 1.00 57.78 ATOM 4142 N LYS H 223 76.586 128.834 217.118 1.00 58.48 ATOM 4143 CA LYS H 223 76.707 127.793 216.105 1.00 58.82 ATOM 4144 CB LYS H 223 77.944 126.928 216.365 1.00 59.91 ATOM 4145 CG LYS H 223 78.155 125.813 215.350 1.00 64.97 ATOM 4146 CD LYS H 223 78.287 126.346 213.928 1.00 72.26 ATOM 4147 CE LYS H 223 79.625 127.044 213.700 1.00 84.90 ATOM 4148 NZ LYS H 223 79.815 127.434 212.268 1.00 83.54 ATOM 4149 C LYS H 223 75.446 126.941 216.050 1.00 55.29 ATOM 4150 O LYS H 223 75.018 126.385 217.054 1.00 51.51 ATOM 4151 N LYS H 224 74.846 126.857 214.871 1.00 56.02 ATOM 4152 CA LYS H 224 73.644 126.061 214.681 1.00 58.48 ATOM 4153 CB LYS H 224 72.858 126.567 213.469 1.00 55.37 ATOM 4154 CG LYS H 224 71.445 126.015 213.354 1.00 56.50 ATOM 4155 CD LYS H 224 70.710 126.648 212.179 1.00 60.02 ATOM 4156 CE LYS H 224 69.404 125.926 211.872 1.00 65.04 ATOM 4157 NZ LYS H 224 68.742 126.484 210.652 1.00 65.46 ATOM 4158 C LYS H 224 74.028 124.596 214.497 1.00 59.68 ATOM 4159 O LYS H 224 74.938 124.277 213.731 1.00 58.47 ATOM 4160 N ALA H 225 73.341 123.714 215.216 1.00 60.11 ATOM 4161 CA ALA H 225 73.608 122.282 215.139 1.00 59.95 ATOM 4162 CB ALA H 225 73.920 121.718 216.527 1.00 56.91 ATOM 4163 C ALA H 225 72.409 121.576 214.532 1.00 60.96 ATOM 4164 O ALA H 225 71.284 121.728 215.004 1.00 61.55 ATOM 4165 N GLU H 226 72.652 120.810 213.474 1.00 63.62 ATOM 4166 CA GLU H 226 71.579 120.107 212.783 1.00 65.91 ATOM 4167 CB GLU H 226 71.022 120.975 211.649 1.00 67.65 ATOM 4168 CG GLU H 226 72.084 121.591 210.750 1.00 67.57 ATOM 4169 CD GLU H 226 71.496 122.501 209.688 1.00 71.24 ATOM 4170 OE1 GLU H 226 72.222 123.395 209.206 1.00 78.78 ATOM 4171 OE2 GLU H 226 70.310 122.326 209.336 1.00 78.34 ATOM 4172 C GLU H 226 72.059 118.761 212.249 1.00 65.84 ATOM 4173 O GLU H 226 73.260 118.559 212.066 1.00 62.89 ATOM 4174 N PRO H 227 71.117 117.830 212.010 1.00 68.35 ATOM 4175 CA PRO H 227 71.407 116.508 211.458 1.00 70.98 ATOM 4176 CB PRO H 227 70.059 116.078 210.892 1.00 72.88 ATOM 4177 CG PRO H 227 69.072 116.707 211.819 1.00 69.68 ATOM 4178 CD PRO H 227 69.677 118.007 212.277 1.00 66.18 ATOM 4179 C PRO H 227 72.465 116.562 210.356 1.00 75.19 ATOM 4180 O PRO H 227 72.351 117.361 209.425 1.00 73.74 ATOM 4181 N LYS H 228 73.476 115.703 210.471 1.00 79.94 ATOM 4182 CA LYS H 228 74.689 115.789 209.647 1.00 83.88 ATOM 4183 CB LYS H 228 75.711 114.714 210.057 1.00 83.61 ATOM 4184 CG LYS H 228 75.124 113.448 210.681 1.00 83.29 ATOM 4185 CD LYS H 228 74.427 112.561 209.656 1.00 86.77 ATOM 4186 CE LYS H 228 74.192 111.164 210.210 1.00 85.41 ATOM 4187 NZ LYS H 228 73.154 110.414 209.454 1.00 81.21 ATOM 4188 C LYS H 228 74.482 115.795 208.127 1.00 86.91 ATOM 4189 O LYS H 228 74.469 114.744 207.490 1.00 87.40 ATOM 4190 N SER H 229 74.327 116.991 207.563 1.00 90.68 ATOM 4191 CA SER H 229 74.294 117.194 206.109 1.00 93.90 ATOM 4192 CB SER H 229 75.673 116.912 205.499 1.00 94.01 ATOM 4193 OG SER H 229 75.709 117.265 204.127 1.00 94.18 ATOM 4194 C SER H 229 73.207 116.411 205.362 1.00 97.04 ATOM 4195 O SER H 229 72.611 116.918 204.408 1.00 97.06 ATOM 4196 N CYS H 230 72.964 115.175 205.787 1.00 99.28 ATOM 4197 CA CYS H 230 71.973 114.319 205.142 1.00 101.38 ATOM 4198 CB CYS H 230 72.594 112.971 204.758 1.00 102.34 ATOM 4199 SG CYS H 230 73.158 111.983 206.169 1.00 107.30 ATOM 4200 C CYS H 230 70.759 114.105 206.043 1.00 101.29 ATOM 4201 O CYS H 230 70.685 114.650 207.145 1.00 100.63 ATOM 4202 N GLU L 1 110.027 113.115 255.998 1.00 79.23 ATOM 4203 CA GLU L 1 108.936 114.100 256.252 1.00 79.03 ATOM 4204 CB GLU L 1 108.971 115.220 255.210 1.00 80.65 ATOM 4205 CG GLU L 1 110.323 115.933 255.149 1.00 87.74 ATOM 4206 CD GLU L 1 110.400 116.974 254.048 1.00 87.24 ATOM 4207 OE1 GLU L 1 109.352 117.571 253.717 1.00 94.85 ATOM 4208 OE2 GLU L 1 111.512 117.196 253.517 1.00 95.93 ATOM 4209 C GLU L 1 107.574 113.414 256.284 1.00 73.20 ATOM 4210 O GLU L 1 107.402 112.339 255.710 1.00 70.47 ATOM 4211 N ILE L 2 106.616 114.044 256.959 1.00 66.98 ATOM 4212 CA ILE L 2 105.338 113.413 257.276 1.00 63.71 ATOM 4213 CB ILE L 2 104.563 114.211 258.352 1.00 64.27 ATOM 4214 CG1 ILE L 2 105.349 114.231 259.665 1.00 65.00 ATOM 4215 CD1 ILE L 2 104.769 115.150 260.725 1.00 62.97 ATOM 4216 CG2 ILE L 2 103.176 113.617 258.564 1.00 57.56 ATOM 4217 C ILE L 2 104.445 113.217 256.059 1.00 63.73 ATOM 4218 O ILE L 2 104.104 114.172 255.369 1.00 67.03 ATOM 4219 N VAL L 3 104.070 111.967 255.811 1.00 61.03 ATOM 4220 CA VAL L 3 103.164 111.627 254.724 1.00 61.04 ATOM 4221 CB VAL L 3 103.772 110.545 253.806 1.00 60.99 ATOM 4222 CG1 VAL L 3 102.750 110.061 252.791 1.00 60.90 ATOM 4223 CG2 VAL L 3 105.010 111.081 253.104 1.00 60.56 ATOM 4224 C VAL L 3 101.843 111.125 255.299 1.00 62.10 ATOM 4225 O VAL L 3 101.822 110.165 256.068 1.00 63.45 ATOM 4226 N LEU L 4 100.751 111.794 254.939 1.00 59.99 ATOM 4227 CA LEU L 4 99.412 111.386 255.356 1.00 59.61 ATOM 4228 CB LEU L 4 98.576 112.604 255.766 1.00 55.51 ATOM 4229 CG LEU L 4 99.079 113.460 256.929 1.00 57.56 ATOM 4230 CD1 LEU L 4 98.077 114.545 257.251 1.00 50.39 ATOM 4231 CD2 LEU L 4 99.335 112.594 258.146 1.00 53.03 ATOM 4232 C LEU L 4 98.699 110.641 254.229 1.00 58.38 ATOM 4233 O LEU L 4 98.685 111.096 253.086 1.00 62.07 ATOM 4234 N THR l 5 98.092 109.510 254.561 1.00 55.82 ATOM 4235 CA THR L 5 97.391 108.695 253.576 1.00 58.62 ATOM 4236 CB THR L 5 98.088 107.333 253.387 1.00 57.76 ATOM 4237 OG1 THR L 5 99.447 107.545 252.991 1.00 61.03 ATOM 4238 CG2 THR L 5 97.379 106.493 252.329 1.00 57.12 ATOM 4239 C THR L 5 95.948 108.466 254.014 1.00 62.05 ATOM 4240 O THR L 5 95.696 107.838 255.042 1.00 63.81 ATOM 4241 N GLN L 6 95.003 108.983 253.238 1.00 63.04 ATOM 4242 CA GLN L 6 93.591 108.820 253.564 1.00 63.68 ATOM 4243 CB GLN L 6 92.810 110.076 253.199 1.00 56.79 ATOM 4244 CG GLN L 6 93.055 111.225 254.156 1.00 58.11 ATOM 4245 CD GLN L 6 92.304 112.480 253.769 1.00 58.16 ATOM 4246 OE1 GLN L 6 92.907 113.463 253.354 1.00 65.95 ATOM 4247 NE2 GLN L 6 90.979 112.452 253.902 1.00 57.03 ATOM 4248 C GLN L 6 92.960 107.609 252.887 1.00 65.83 ATOM 4249 O GLN L 6 93.376 107.194 251.806 1.00 68.12 ATOM 4250 N SER L 7 91.964 107.033 253.546 1.00 63.33 ATOM 4251 CA SER L 7 91.144 106.005 252.931 1.00 62.88 ATOM 4252 CB SER L 7 91.741 104.604 253.139 1.00 58.30 ATOM 4253 OG SER L 7 91.488 104.109 254.441 1.00 69.20 ATOM 4254 C SER L 7 89.720 106.102 253.476 1.00 61.60 ATOM 4255 O SER L 7 89.506 106.613 254.582 1.00 60.23 ATOM 4256 N PRO L 8 88.737 105.660 252.679 1.00 61.67 ATOM 4257 CA PRO L 8 88.942 105.236 251.296 1.00 61.33 ATOM 4258 CB PRO L 8 87.653 104.478 250.977 1.00 64.15 ATOM 4259 CG PRO L 8 86.622 105.130 251.833 1.00 63.78 ATOM 4260 CD PRO L 8 87.330 105.531 253.101 1.00 60.62 ATOM 4261 C PRO L 8 89.094 106.442 250.362 1.00 63.99 ATOM 4262 O PRO L 8 88.859 107.576 250.778 1.00 66.24 ATOM 4263 N GLY L 9 89.496 106.201 249.119 1.00 59.30 ATOM 4264 CA GLY L 9 89.597 107.275 248.137 1.00 60.54 ATOM 4265 C GLY L 9 88.247 107.910 247.865 1.00 60.76 ATOM 4266 O GLY L 9 88.138 109.127 247.711 1.00 64.02 ATOM 4267 N THR L 10 87.217 107.073 247.806 1.00 64.00 ATOM 4268 CA THR L 10 85.851 107.523 247.579 1.00 64.54 ATOM 4269 CB THR L 10 85.384 107.221 246.133 1.00 66.35 ATOM 4270 OG1 THR L 10 86.074 108.071 245.207 1.00 60.28 ATOM 4271 CG2 THR L 10 83.886 107.439 245.990 1.00 66.83 ATOM 4272 C THR L 10 84.932 106.809 248.560 1.00 65.31 ATOM 4273 O THR L 10 85.017 105.599 248.736 1.00 65.80 ATOM 4274 N LEU L 11 84.062 107.570 249.208 1.00 66.21 ATOM 4275 CA LEU L 11 83.079 107.010 250.119 1.00 66.16 ATOM 4276 CB LEU L 11 83.206 107.673 251.496 1.00 64.77 ATOM 4277 CG LEU L 11 82.612 107.012 252.737 1.00 64.65 ATOM 4278 CD1 LEU L 11 83.123 105.594 252.916 1.00 65.72 ATOM 4279 CD2 LEU L 11 82.929 107.845 253.968 1.00 72.90 ATOM 4280 C LEU L 11 81.710 107.278 249.506 1.00 66.08 ATOM 4281 O LEU L 11 81.327 108.434 249.307 1.00 69.40 ATOM 4282 N SER L 12 80.989 106.214 249.172 1.00 61.72 ATOM 4283 CA SER L 12 79.682 106.350 248.543 1.00 62.27 ATOM 4284 CB SER L 12 79.583 105.438 247.319 1.00 60.88 ATOM 4285 OG SER L 12 80.711 105.593 246.481 1.00 61.92 ATOM 4286 C SER L 12 78.582 105.992 249.523 1.00 62.88 ATOM 4287 O SER L 12 78.414 104.820 249.867 1.00 59.94 ATOM 4288 N LEU L 13 77.823 106.992 249.964 1.00 60.84 ATOM 4289 CA LEU L 13 76.768 106.746 250.952 1.00 59.83 ATOM 4290 CB LEU L 13 77.235 107.156 252.349 1.00 56.40 ATOM 4291 CG LEU L 13 78.491 106.460 252.878 1.00 63.43 ATOM 4292 CD1 LEU L 13 79.049 107.243 254.039 1.00 63.74 ATOM 4293 CD2 LEU L 13 78.217 105.010 253.275 1.00 58.96 ATOM 4294 C LEU L 13 75.455 107.447 250.628 1.00 58.48 ATOM 4295 O LEU L 13 75.421 108.428 249.887 1.00 61.65 ATOM 4296 N SER L 14 74.373 106.920 251.183 1.00 58.44 ATOM 4297 CA SER L 14 73.069 107.557 251.088 1.00 60.32 ATOM 4298 CB SER L 14 71.968 106.496 251.043 1.00 59.67 ATOM 4299 OG SER L 14 72.092 105.696 249.883 1.00 68.85 ATOM 4300 C SER L 14 72.871 108.448 252.306 1.00 60.92 ATOM 4301 O SER L 14 73.463 108.201 253.360 1.00 62.19 ATOM 4302 N PRO L 15 72.039 109.491 252.171 1.00 60.99 ATOM 4303 CA PRO L 15 71.725 110.297 253.346 1.00 59.39 ATOM 4304 CB PRO L 15 70.644 111.253 252.837 1.00 59.60 ATOM 4305 CG PRO L 15 70.879 111.341 251.357 1.00 63.74 ATOM 4306 CD PRO L 15 71.352 109.973 250.957 1.00 59.83 ATOM 4307 C PRO L 15 71.168 109.406 254.453 1.00 58.57 ATOM 4308 O PRO L 15 70.375 108.512 254.180 1.00 59.10 ATOM 4309 N GLY L 16 71.593 109.642 255.688 1.00 61.37 ATOM 4310 CA GLY L 16 71.121 108.856 256.819 1.00 59.77 ATOM 4311 C GLY L 16 72.131 107.822 257.276 1.00 60.53 ATOM 4312 O GLY L 16 72.065 107.345 258.402 1.00 57.45 ATOM 4313 N GLU L 17 73.067 107.473 256.397 1.00 62.67 ATOM 4314 CA GLU L 17 74.088 106.478 256.718 1.00 63.70 ATOM 4315 CB GLU L 17 74.578 105.764 255.454 1.00 62.74 ATOM 4316 CG GLU L 17 73.644 104.702 254.916 1.00 59.77 ATOM 4317 CD GLU L 17 74.248 103.940 253.747 1.00 66.34 ATOM 4318 OE1 GLU L 17 74.445 104.543 252.671 1.00 71.02 ATOM 4319 OE2 GLU L 17 74.526 102.733 253.901 1.00 77.06 ATOM 4320 C GLU L 17 75.276 107.096 257.440 1.00 65.20 ATOM 4321 O GLU L 17 75.570 108.283 257.285 1.00 68.70 ATOM 4322 N ARG L 18 75.962 106.272 258.222 1.00 65.53 ATOM 4323 CA ARG L 18 77.151 106.683 258.954 1.00 63.81 ATOM 4324 CB ARG L 18 77.409 105.689 260.088 1.00 66.39 ATOM 4325 CG ARG L 18 78.577 106.011 261.003 1.00 66.80 ATOM 4326 CD ARG L 18 78.803 104.839 261.933 1.00 67.10 ATOM 4327 NE ARG L 18 79.835 105.083 262.932 1.00 73.84 ATOM 4328 CZ ARG L 18 79.633 105.745 264.067 1.00 77.50 ATOM 4329 NH1 ARG L 18 78.436 106.250 264.340 1.00 74.63 ATOM 4330 NH2 ARG L 18 80.630 105.911 264.925 1.00 75.24 ATOM 4331 C ARG L 18 78.344 106.722 258.008 1.00 64.07 ATOM 4332 O ARG L 18 78.474 105.860 257.137 1.00 62.13 ATOM 4333 N ALA L 19 79.203 107.727 258.175 1.00 63.60 ATOM 4334 CA ALA L 19 80.435 107.851 257.395 1.00 61.13 ATOM 4335 CB ALA L 19 80.427 109.134 256.588 1.00 62.57 ATOM 4336 C ALA L 19 81.673 107.802 258.291 1.00 64.12 ATOM 4337 O ALA L 19 81.685 108.384 259.379 1.00 67.45 ATOM 4338 N THR L 20 82.708 107.107 257.829 1.00 62.45 ATOM 4339 CA THR L 20 83.961 106.981 258.567 1.00 61.87 ATOM 4340 CB THR L 20 84.116 105.572 259.179 1.00 67.35 ATOM 4341 OG1 THR L 20 83.049 105.325 260.108 1.00 67.34 ATOM 4342 CG2 THR L 20 85.453 105.442 259.905 1.00 64.47 ATOM 4343 C THR L 20 85.141 107.254 257.643 1.00 63.29 ATOM 4344 O THR L 20 85.382 106.502 256.705 1.00 65.79 ATOM 4345 N PHE L 21 85.860 108.344 257.898 1.00 66.77 ATOM 4346 CA PHE L 21 87.046 108.695 257.121 1.00 65.45 ATOM 4347 CB PHE L 21 87.106 110.201 256.857 1.00 66.16 ATOM 4348 CG PHE L 21 85.921 110.748 256.124 1.00 59.10 ATOM 4349 CD1 PHE L 21 86.006 111.046 254.778 1.00 64.76 ATOM 4350 CE1 PHE L 21 84.920 111.566 254.095 1.00 68.54 ATOM 4351 CZ PHE L 21 83.731 111.791 254.763 1.00 62.41 ATOM 4352 CE2 PHE L 21 83.637 111.508 256.109 1.00 63.07 ATOM 4353 CD2 PHE L 21 84.730 110.990 256.785 1.00 61.71 ATOM 4354 C PHE L 21 88.285 108.318 257.916 1.00 66.37 ATOM 4355 O PHE L 21 88.378 108.641 259.100 1.00 65.13 ATOM 4356 N SER L 22 89.238 107.654 257.263 1.00 63.09 ATOM 4357 CA SER L 22 90.500 107.284 257.906 1.00 59.64 ATOM 4358 CB SER L 22 90.840 105.816 257.634 1.00 57.27 ATOM 4359 OG SER L 22 89.984 104.956 258.354 1.00 62.71 ATOM 4360 C SER L 22 91.657 108.144 257.430 1.00 55.37 ATOM 4361 O SER L 22 91.782 108.422 256.242 1.00 56.20 ATOM 4362 N CYS L 23 92.504 108.553 258.367 1.00 60.10 ATOM 4363 CA CYS L 23 93.757 109.226 258.046 1.00 60.05 ATOM 4364 CB CYS L 23 93.698 110.701 258.434 1.00 63.91 ATOM 4365 SG CYS L 23 95.182 111.651 258.027 1.00 72.43 ATOM 4366 C CYS L 23 94.892 108.529 258.786 1.00 63.01 ATOM 4367 O CYS L 23 94.847 108.366 260.008 1.00 63.40 ATOM 4368 N ARG L 24 95.902 108.106 258.039 1.00 60.56 ATOM 4369 CA ARG L 24 97.036 107.404 258.614 1.00 62.36 ATOM 4370 CB ARG L 24 97.098 105.981 258.048 1.00 59.88 ATOM 4371 CG ARG L 24 98.126 105.068 258.688 1.00 75.93 ATOM 4372 CD ARG L 24 99.329 104.867 257.778 1.00 88.35 ATOM 4373 NE ARG L 24 98.924 104.536 256.414 1.00 96.88 ATOM 4374 CZ ARG L 24 99.738 104.039 255.486 1.00 97.96 ATOM 4375 NH1 ARG L 24 99.274 103.774 254.271 1.00 95.44 ATOM 4376 NH2 ARG L 24 101.012 103.804 255.772 1.00 97.25 ATOM 4377 C ARG L 24 98.310 108.189 258.313 1.00 61.06 ATOM 4378 O ARG L 24 98.523 108.610 257.179 1.00 63.31 ATOM 4379 N SER L 25 99.142 108.414 259.329 1.00 57.41 ATOM 4380 CA SER L 25 100.401 109.126 259.117 1.00 59.33 ATOM 4381 CB SER L 25 100.542 110.323 260.064 1.00 58.38 ATOM 4382 OG SER L 25 100.521 109.924 261.417 1.00 71.02 ATOM 4383 C SER L 25 101.611 108.213 259.245 1.00 60.18 ATOM 4384 O SER L 25 101.596 107.252 260.010 1.00 60.62 ATOM 4385 N SER L 26 102.652 108.522 258.477 1.00 58.25 ATOM 4386 CA SER L 26 103.909 107.796 258.531 1.00 57.76 ATOM 4387 CB SER L 26 104.800 108.219 257.365 1.00 57.93 ATOM 4388 OG SER L 26 104.842 109.632 257.258 1.00 62.34 ATOM 4389 C SER L 26 104.625 108.065 259.850 1.00 59.28 ATOM 4390 O SER L 26 105.576 107.366 260.206 1.00 60.11 ATOM 4391 N HIS L 27 104.160 109.084 260.567 1.00 56.78 ATOM 4392 CA HIS L 27 104.752 109.487 261.837 1.00 57.16 ATOM 4393 CB HIS L 27 105.475 110.830 261.690 1.00 55.30 ATOM 4394 CG HIS L 27 106.598 110.809 260.701 1.00 58.40 ATOM 4395 ND1 HIS L 27 107.923 110.866 261.078 1.00 58.86 ATOM 4396 CE1 HIS L 27 108.686 110.831 260.001 1.00 55.82 ATOM 4397 NE2 HIS L 27 107.905 110.748 258.939 1.00 66.43 ATOM 4398 CD2 HIS L 27 106.594 110.734 259.350 1.00 54.96 ATOM 4399 C HIS L 27 103.686 109.621 262.915 1.00 58.26 ATOM 4400 O HIS L 27 102.587 110.112 262.654 1.00 58.41 ATOM 4401 N SER L 28 104.019 109.193 264.127 1.00 58.33 ATOM 4402 CA SER L 28 103.152 109.396 265.276 1.00 59.64 ATOM 4403 CB SER L 28 103.738 108.697 266.499 1.00 59.35 ATOM 4404 OG SER L 28 102.769 108.536 267.517 1.00 64.61 ATOM 4405 C SER L 28 103.016 110.892 265.543 1.00 60.72 ATOM 4406 O SER L 28 104.011 111.589 265.742 1.00 64.18 ATOM 4407 N ILE L 29 101.783 111.384 265.537 1.00 61.55 ATOM 4408 CA ILE L 29 101.527 112.808 265.719 1.00 61.14 ATOM 4409 CB ILE L 29 100.314 113.272 264.883 1.00 58.31 ATOM 4410 CG1 ILE L 29 100.454 112.799 263.432 1.00 57.79 ATOM 4411 CD1 ILE L 29 101.705 113.292 262.726 1.00 53.88 ATOM 4412 CG2 ILE L 29 100.160 114.782 264.937 1.00 56.20 ATOM 4413 C ILE L 29 101.322 113.132 267.202 1.00 64.63 ATOM 4414 O ILE L 29 100.190 113.242 267.685 1.00 64.41 ATOM 4415 N ARG L 30 102.435 113.280 267.914 1.00 64.60 ATOM 4416 CA ARG L 30 102.416 113.507 269.357 1.00 67.99 ATOM 4417 CB ARG L 30 103.838 113.458 269.928 1.00 71.35 ATOM 4418 CG ARG L 30 104.887 114.131 269.052 1.00 80.22 ATOM 4419 CD ARG L 30 105.676 113.114 268.229 1.00 84.35 ATOM 4420 NE ARG L 30 106.796 112.559 268.984 1.00 76.99 ATOM 4421 CZ ARG L 30 107.988 113.140 269.080 1.00 75.98 ATOM 4422 NH1 ARG L 30 108.954 112.573 269.788 1.00 73.10 ATOM 4423 NH2 ARG L 30 108.214 114.293 268.467 1.00 87.55 ATOM 4424 C ARG L 30 101.746 114.817 269.760 1.00 64.73 ATOM 4425 O ARG L 30 101.145 114.908 270.828 1.00 66.84 ATOM 4426 N SER L 31 101.855 115.827 268.904 1.00 62.65 ATOM 4427 CA SER L 31 101.321 117.151 269.204 1.00 61.53 ATOM 4428 CB SER L 31 101.843 118.168 268.195 1.00 59.84 ATOM 4429 OG SER L 31 101.284 117.917 266.918 1.00 64.81 ATOM 4430 C SER L 31 99.801 117.172 269.195 1.00 59.84 ATOM 4431 O SER L 31 99.188 118.101 269.711 1.00 68.94 ATOM 4432 N ARG L 32 99.198 116.142 268.611 1.00 59.16 ATOM 4433 CA ARG L 32 97.747 116.089 268.425 1.00 58.01 ATOM 4434 CB ARG L 32 97.017 116.072 269.767 1.00 57.75 ATOM 4435 CG ARG L 32 97.215 114.768 270.532 1.00 59.78 ATOM 4436 CD ARG L 32 96.359 114.711 271.773 1.00 62.48 ATOM 4437 NE ARG L 32 94.931 114.771 271.476 1.00 68.67 ATOM 4438 CZ ARG L 32 94.167 113.706 271.254 1.00 65.43 ATOM 4439 NH1 ARG L 32 94.694 112.490 271.284 1.00 62.96 ATOM 4440 NH2 ARG L 32 92.875 113.861 270.996 1.00 72.48 ATOM 4441 C ARG L 32 97.239 117.223 267.536 1.00 59.09 ATOM 4442 O ARG L 32 96.054 117.559 267.548 1.00 64.08 ATOM 4443 N ARG L 33 98.146 117.800 266.757 1.00 59.16 ATOM 4444 CA ARG L 33 97.793 118.859 265.822 1.00 59.00 ATOM 4445 CB ARG L 33 98.966 119.824 265.636 1.00 59.46 ATOM 4446 CG ARG L 33 99.291 120.611 266.897 1.00 57.89 ATOM 4447 CD ARG L 33 100.171 121.805 266.608 1.00 58.44 ATOM 4448 NE ARG L 33 101.593 121.489 266.687 1.00 68.83 ATOM 4449 CZ ARG L 33 102.413 121.958 267.623 1.00 67.09 ATOM 4450 NH1 ARG L 33 101.962 122.768 268.573 1.00 68.70 ATOM 4451 NH2 ARG L 33 103.692 121.615 267.608 1.00 80.04 ATOM 4452 C ARG L 33 97.331 118.283 264.484 1.00 61.50 ATOM 4453 O ARG L 33 98.029 118.380 263.472 1.00 59.55 ATOM 4454 N VAL L 34 96.144 117.677 264.508 1.00 60.26 ATOM 4455 CA VAL L 34 95.502 117.111 263.325 1.00 58.30 ATOM 4456 CB VAL L 34 95.178 115.611 263.537 1.00 58.96 ATOM 4457 CG1 VAL L 34 94.498 115.024 262.315 1.00 54.15 ATOM 4458 CG2 VAL L 34 96.442 114.827 263.875 1.00 52.60 ATOM 4459 C VAL L 34 94.197 117.857 263.035 1.00 60.98 ATOM 4460 O VAL L 34 93.379 118.078 263.933 1.00 58.00 ATOM 4461 N ALA L 35 94.003 118.257 261.787 1.00 60.45 ATOM 4462 CA ALA L 35 92.779 118.935 261.405 1.00 60.41 ATOM 4463 CB ALA L 35 93.059 120.397 261.089 1.00 63.72 ATOM 4464 C ALA L 35 92.109 118.247 260.216 1.00 66.00 ATOM 4465 O ALA L 35 92.758 117.536 259.435 1.00 63.88 ATOM 4466 N TRP L 36 90.805 118.467 260.089 1.00 62.62 ATOM 4467 CA TRP L 36 90.041 117.968 258.955 1.00 61.21 ATOM 4468 CB TRP L 36 88.959 116.986 259.414 1.00 60.48 ATOM 4469 CG TRP L 36 89.485 115.670 259.902 1.00 60.41 ATOM 4470 CD1 TRP L 36 89.851 115.353 261.178 1.00 56.69 ATOM 4471 NE1 TRP L 36 90.278 114.050 261.239 1.00 59.19 ATOM 4472 CE2 TRP L 36 90.190 113.496 259.988 1.00 64.55 ATOM 4473 CD2 TRP L 36 89.691 114.487 259.121 1.00 63.09 ATOM 4474 CE3 TRP L 36 89.497 114.171 257.773 1.00 63.13 ATOM 4475 CZ3 TRP L 36 89.811 112.891 257.338 1.00 55.29 ATOM 4476 CH2 TRP L 36 90.304 111.925 258.228 1.00 64.11 ATOM 4477 CZ2 TRP L 36 90.496 112.207 259.553 1.00 63.99 ATOM 4478 C TRP L 36 89.387 119.147 258.274 1.00 60.67 ATOM 4479 O TRP L 36 88.907 120.060 258.947 1.00 60.35 ATOM 4480 N TYR L 37 89.376 119.121 256.945 1.00 60.18 ATOM 4481 CA TYR L 37 88.774 120.175 256.145 1.00 61.73 ATOM 4482 CB TYR L 37 89.851 120.958 255.375 1.00 62.27 ATOM 4483 CG TYR L 37 90.886 121.596 256.280 1.00 63.87 ATOM 4484 CD1 TYR L 37 92.061 120.928 256.607 1.00 61.52 ATOM 4485 CE1 TYR L 37 93.005 121.507 257.445 1.00 60.03 ATOM 4486 CZ TYR L 37 92.776 122.768 257.964 1.00 64.32 ATOM 4487 OH TYR L 37 93.705 123.358 258.800 1.00 59.71 ATOM 4488 CE2 TYR L 37 91.615 123.445 257.655 1.00 54.36 ATOM 4489 CD2 TYR L 37 90.679 122.860 256.819 1.00 66.04 ATOM 4490 C TYR L 37 87.740 119.608 255.174 1.00 63.57 ATOM 4491 O TYR L 37 87.877 118.488 254.667 1.00 63.69 ATOM 4492 N GLN L 38 86.694 120.387 254.937 1.00 64.85 ATOM 4493 CA GLN L 38 85.694 120.060 253.937 1.00 57.98 ATOM 4494 CB GLN L 38 84.295 120.210 254.531 1.00 63.53 ATOM 4495 CG GLN L 38 83.150 119.842 253.598 1.00 63.85 ATOM 4496 CD GLN L 38 81.818 120.332 254.123 1.00 71.13 ATOM 4497 OE1 GLN L 38 81.514 121.523 254.043 1.00 66.66 ATOM 4498 NE2 GLN L 38 81.013 119.415 254.670 1.00 59.25 ATOM 4499 C GLN L 38 85.883 121.022 252.780 1.00 63.52 ATOM 4500 O GLN L 38 86.081 122.224 252.982 1.00 64.21 ATOM 4501 N HIS L 39 85.846 120.497 251.562 1.00 62.62 ATOM 4502 CA HIS L 39 86.007 121.342 250.390 1.00 60.50 ATOM 4503 CB HIS L 39 87.425 121.221 249.818 1.00 57.40 ATOM 4504 CG HIS L 39 87.751 122.267 248.798 1.00 59.58 ATOM 4505 ND1 HIS L 39 88.781 122.133 247.890 1.00 60.80 ATOM 4506 CE1 HIS L 39 88.826 123.203 247.118 1.00 66.03 ATOM 4507 NE2 HIS L 39 87.856 124.023 247.484 1.00 63.23 ATOM 4508 CD2 HIS L 39 87.170 123.461 248.533 1.00 64.72 ATOM 4509 C HIS L 39 84.972 121.016 249.321 1.00 60.57 ATOM 4510 O HIS L 39 84.887 119.883 248.863 1.00 60.04 ATOM 4511 N LYS L 40 84.184 122.018 248.943 1.00 65.35 ATOM 4512 CA LYS L 40 83.217 121.887 247.858 1.00 66.19 ATOM 4513 CB LYS L 40 81.826 122.330 248.322 1.00 64.95 ATOM 4514 CG LYS L 40 81.226 121.457 249.422 1.00 69.10 ATOM 4515 CD LYS L 40 79.851 121.950 249.825 1.00 66.70 ATOM 4516 CE LYS L 40 79.353 121.216 251.051 1.00 75.93 ATOM 4517 NZ LYS L 40 78.217 121.934 251.694 1.00 69.56 ATOM 4518 C LYS L 40 83.668 122.739 246.676 1.00 69.59 ATOM 4519 O LYS L 40 84.227 123.819 246.869 1.00 68.51 ATOM 4520 N PRO L 41 83.406 122.262 245.448 1.00 73.27 ATOM 4521 CA PRO L 41 83.897 122.873 244.208 1.00 73.22 ATOM 4522 CB PRO L 41 83.182 122.070 243.109 1.00 75.81 ATOM 4523 CG PRO L 41 82.053 121.352 243.806 1.00 74.78 ATOM 4524 CD PRO L 41 82.572 121.078 245.178 1.00 74.14 ATOM 4525 C PRO L 41 83.524 124.342 244.086 1.00 71.93 ATOM 4526 O PRO L 41 82.346 124.682 244.130 1.00 73.30 ATOM 4527 N GLY L 42 84.524 125.202 243.939 1.00 72.22 ATOM 4528 CA GLY L 42 84.279 126.630 243.764 1.00 70.68 ATOM 4529 C GLY L 42 84.083 127.364 245.073 1.00 67.85 ATOM 4530 O GLY L 42 83.818 128.567 245.087 1.00 69.99 ATOM 4531 N GLN L 43 84.218 126.640 246.180 1.00 66.45 ATOM 4532 CA GLN L 43 84.005 127.218 247.498 1.00 63.91 ATOM 4533 CB GLN L 43 82.849 126.509 248.212 1.00 62.66 ATOM 4534 CG GLN L 43 81.509 126.627 247.496 1.00 64.25 ATOM 4535 CD GLN L 43 80.354 125.989 248.263 1.00 62.82 ATOM 4536 OE1 GLN L 43 79.611 125.177 247.714 1.00 76.76 ATOM 4537 NE2 GLN L 43 80.194 126.361 249.528 1.00 61.89 ATOM 4538 C GLN L 43 85.277 127.142 248.336 1.00 63.26 ATOM 4539 O GLN L 43 86.081 126.225 248.174 1.00 61.38 ATOM 4540 N ALA L 44 85.458 128.118 249.221 1.00 63.26 ATOM 4541 CA ALA L 44 86.568 128.102 250.162 1.00 57.03 ATOM 4542 CB ALA L 44 86.501 129.308 251.058 1.00 57.51 ATOM 4543 C ALA L 44 86.515 126.827 250.990 1.00 59.52 ATOM 4544 O ALA L 44 85.439 126.422 251.431 1.00 60.09 ATOM 4545 N PRO L 45 87.670 126.166 251.184 1.00 60.82 ATOM 4546 CA PRO L 45 87.677 125.022 252.100 1.00 62.49 ATOM 4547 CB PRO L 45 89.146 124.590 252.120 1.00 57.89 ATOM 4548 CG PRO L 45 89.678 125.063 250.820 1.00 58.69 ATOM 4549 CD PRO L 45 88.995 126.391 250.589 1.00 57.38 ATOM 4550 C PRO L 45 87.235 125.465 253.484 1.00 60.92 ATOM 4551 O PRO L 45 87.362 126.638 253.822 1.00 61.31 ATOM 4552 N ARG L 46 86.708 124.534 254.269 1.00 62.88 ATOM 4553 CA ARG L 46 86.167 124.862 255.574 1.00 62.44 ATOM 4554 CB ARG L 46 84.640 124.759 255.565 1.00 60.67 ATOM 4555 CG ARG L 46 84.034 125.029 256.926 1.00 76.99 ATOM 4556 CD ARG L 46 82.530 125.187 256.897 1.00 85.02 ATOM 4557 NE ARG L 46 82.079 125.905 258.088 1.00 96.48 ATOM 4558 CZ ARG L 46 80.850 125.842 258.591 1.00 95.01 ATOM 4559 NH1 ARG L 46 79.926 125.082 258.018 1.00 95.27 ATOM 4560 NH2 ARG L 46 80.549 126.536 259.678 1.00 99.19 ATOM 4561 C ARG L 46 86.737 123.950 256.645 1.00 65.72 ATOM 4562 O ARG L 46 86.791 122.732 256.465 1.00 65.23 ATOM 4563 N LEU L 47 87.168 124.540 257.758 1.00 62.41 ATOM 4564 CA LEU L 47 87.664 123.762 258.888 1.00 61.23 ATOM 4565 CB LEU L 47 88.317 124.680 259.928 1.00 59.11 ATOM 4566 CG LEU L 47 88.896 123.986 261.163 1.00 58.22 ATOM 4567 CD1 LEU L 47 90.163 123.217 260.804 1.00 57.93 ATOM 4568 CD2 LEU L 47 89.164 124.959 262.312 1.00 55.47 ATOM 4569 C LEU L 47 86.516 122.996 259.532 1.00 61.91 ATOM 4570 O LEU L 47 85.466 123.572 259.839 1.00 60.69 ATOM 4571 N VAL L 48 86.710 121.700 259.735 1.00 59.43 ATOM 4572 CA VAL L 48 85.697 120.883 260.394 1.00 62.66 ATOM 4573 CB VAL L 48 85.371 119.604 259.591 1.00 62.71 ATOM 4574 CG1 VAL L 48 84.278 118.809 260.290 1.00 55.85 ATOM 4575 CG2 VAL L 48 84.964 119.952 258.179 1.00 64.61 ATOM 4576 C VAL L 48 86.138 120.483 261.805 1.00 59.86 ATOM 4577 O VAL L 48 85.386 120.638 262.768 1.00 62.01 ATOM 4578 N ILE L 49 87.363 119.976 261.909 1.00 60.62 ATOM 4579 CA ILE L 49 87.940 119.528 263.170 1.00 57.86 ATOM 4580 CB ILE L 49 88.068 117.986 263.218 1.00 60.21 ATOM 4581 CG1 ILE L 49 86.698 117.304 263.153 1.00 60.81 ATOM 4582 CD1 ILE L 49 85.841 117.490 264.406 1.00 56.83 ATOM 4583 CG2 ILE L 49 88.814 117.558 264.465 1.00 59.47 ATOM 4584 C ILE L 49 89.349 120.094 263.336 1.00 63.74 ATOM 4585 O ILE L 49 90.114 120.160 262.370 1.00 65.87 ATOM 4586 N HIS L 50 89.696 120.490 264.560 1.00 64.10 ATOM 4587 CA HIS L 50 91.085 120.805 264.892 1.00 59.77 ATOM 4588 CB HIS L 50 91.330 122.316 264.944 1.00 60.20 ATOM 4589 CG HIS L 50 90.527 123.037 265.982 1.00 63.13 ATOM 4590 ND1 HIS L 50 90.966 123.209 267.278 1.00 65.78 ATOM 4591 CE1 HIS L 50 90.067 123.898 267.959 1.00 53.43 ATOM 4592 NE2 HIS L 50 89.058 124.175 267.153 1.00 55.81 ATOM 4593 CD2 HIS L 50 89.326 123.658 265.907 1.00 53.74 ATOM 4594 C HIS L 50 91.495 120.123 266.190 1.00 58.85 ATOM 4595 O HIS L 50 90.644 119.680 266.962 1.00 58.29 ATOM 4596 N GLY L 51 92.799 120.018 266.425 1.00 60.07 ATOM 4597 CA GLY L 51 93.297 119.342 267.622 1.00 59.85 ATOM 4598 C GLY L 51 92.765 117.925 267.742 1.00 63.88 ATOM 4599 O GLY L 51 92.382 117.481 268.829 1.00 63.66 ATOM 4600 N VAL L 52 92.731 117.221 266.614 1.00 63.03 ATOM 4601 CA VAL L 52 92.216 115.847 266.543 1.00 64.21 ATOM 4602 CB VAL L 52 92.957 114.887 267.511 1.00 63.66 ATOM 4603 CG1 VAL L 52 92.298 113.512 267.518 1.00 59.50 ATOM 4604 CG2 VAL L 52 94.420 114.767 267.121 1.00 54.39 ATOM 4605 C VAL L 52 90.699 115.728 266.748 1.00 66.44 ATOM 4606 O VAL L 52 90.015 115.066 265.953 1.00 60.80 ATOM 4607 N SER L 53 90.179 116.377 267.792 1.00 61.35 ATOM 4608 CA SER L 53 88.797 116.143 268.223 1.00 63.96 ATOM 4609 CB SER L 53 88.778 115.272 269.486 1.00 61.09 ATOM 4610 OG SER L 53 89.583 115.832 270.504 1.00 70.86 ATOM 4611 C SER L 53 87.927 117.374 268.464 1.00 61.54 ATOM 4612 O SER L 53 86.757 117.231 268.815 1.00 61.32 ATOM 4613 N ASN L 54 88.481 118.571 268.293 1.00 59.31 ATOM 4614 CA ASN L 54 87.702 119.784 268.516 1.00 60.59 ATOM 4615 CB ASN L 54 88.599 120.940 268.940 1.00 63.60 ATOM 4616 CG ASN L 54 89.371 120.637 270.193 1.00 62.96 ATOM 4617 OD1 ASN L 54 88.791 120.372 271.243 1.00 68.63 ATOM 4618 ND2 ASN L 54 90.692 120.670 270.092 1.00 67.79 ATOM 4619 C ASN L 54 86.877 120.192 267.302 1.00 63.00 ATOM 4620 O ASN L 54 87.416 120.501 266.239 1.00 60.29 ATOM 4621 N ARG L 55 85.563 120.196 267.478 1.00 62.58 ATOM 4622 CA ARG L 55 84.647 120.621 266.439 1.00 62.84 ATOM 4623 CB ARG L 55 83.222 120.296 266.862 1.00 64.63 ATOM 4624 CG ARG L 55 82.197 120.410 265.772 1.00 66.27 ATOM 4625 CD ARG L 55 80.852 119.915 266.268 1.00 72.65 ATOM 4626 NE ARG L 55 80.901 118.493 266.572 1.00 66.33 ATOM 4627 CZ ARG L 55 80.640 117.959 267.762 1.00 64.01 ATOM 4628 NH1 ARG L 55 80.280 118.724 268.782 1.00 58.83 ATOM 4629 NH2 ARG L 55 80.721 116.645 267.921 1.00 58.72 ATOM 4630 C ARG L 55 84.800 122.118 266.200 1.00 63.96 ATOM 4631 O ARG L 55 84.749 122.909 267.142 1.00 63.12 ATOM 4632 N ALA L 56 84.997 122.504 264.941 1.00 61.57 ATOM 4633 CA ALA L 56 85.175 123.910 264.598 1.00 60.83 ATOM 4634 CB ALA L 56 85.763 124.042 263.211 1.00 59.13 ATOM 4635 C ALA L 56 83.844 124.650 264.689 1.00 62.17 ATOM 4636 O ALA L 56 82.783 124.025 264.707 1.00 60.25 ATOM 4637 N SER L 57 83.900 125.978 264.743 1.00 61.72 ATOM 4638 CA SER L 57 82.692 126.782 264.915 1.00 65.81 ATOM 4639 CB SER L 57 83.046 128.255 265.135 1.00 71.73 ATOM 4640 OG SER L 57 84.198 128.612 264.390 1.00 83.27 ATOM 4641 C SER L 57 81.710 126.642 263.759 1.00 61.69 ATOM 4642 O SER L 57 82.096 126.688 262.592 1.00 65.84 ATOM 4643 N GLY L 58 80.438 126.462 264.102 1.00 62.99 ATOM 4644 CA GLY L 58 79.365 126.364 263.123 1.00 61.57 ATOM 4645 C GLY L 58 79.155 124.958 262.605 1.00 63.67 ATOM 4646 O GLY L 58 78.207 124.700 261.866 1.00 66.74 ATOM 4647 N ILE L 59 80.042 124.044 262.986 1.00 61.61 ATOM 4648 CA ILE L 59 79.999 122.676 262.467 1.00 59.26 ATOM 4649 CB ILE L 59 81.397 121.999 262.535 1.00 57.98 ATOM 4650 CG1 ILE L 59 82.418 122.764 261.674 1.00 55.56 ATOM 4651 CD1 ILE L 59 82.071 122.849 260.184 1.00 47.78 ATOM 4652 CG2 ILE L 59 81.319 120.530 262.129 1.00 60.09 ATOM 4653 C ILE L 59 78.951 121.833 263.201 1.00 59.12 ATOM 4654 O ILE L 59 78.888 121.832 264.428 1.00 58.91 ATOM 4655 N SER L 60 78.126 121.129 262.433 1.00 57.42 ATOM 4656 CA SER L 60 77.079 120.282 262.980 1.00 56.19 ATOM 4657 CB SER L 60 76.349 119.568 261.843 1.00 53.43 ATOM 4658 OG SER L 60 75.455 118.592 262.351 1.00 56.21 ATOM 4659 C SER L 60 77.644 119.246 263.947 1.00 59.03 ATOM 4660 O SER L 60 78.724 118.699 263.715 1.00 59.78 ATOM 4661 N ASP L 61 76.900 118.963 265.016 1.00 57.44 ATOM 4662 CA ASP L 61 77.320 117.965 266.004 1.00 58.11 ATOM 4663 CB ASP L 61 76.506 118.085 267.300 1.00 55.97 ATOM 4664 CG ASP L 61 75.026 117.825 267.096 1.00 53.24 ATOM 4665 OD1 ASP L 61 74.633 117.360 266.006 1.00 53.85 ATOM 4666 OD2 ASP L 61 74.250 118.088 268.038 1.00 50.08 ATOM 4667 C ASP L 61 77.284 116.528 265.482 1.00 60.78 ATOM 4668 O ASP L 61 77.597 115.595 266.217 1.00 61.86 ATOM 4669 N ARG L 62 76.899 116.354 264.219 1.00 60.96 ATOM 4670 CA ARG L 62 76.980 115.051 263.559 1.00 62.95 ATOM 4671 CB ARG L 62 76.167 115.043 262.259 1.00 63.38 ATOM 4672 CG ARG L 62 74.659 115.086 262.446 1.00 65.81 ATOM 4673 CD ARG L 62 73.930 115.209 261.104 1.00 64.14 ATOM 4674 NE ARG L 62 74.281 116.433 260.384 1.00 61.25 ATOM 4675 CZ ARG L 62 75.053 116.471 259.302 1.00 63.39 ATOM 4676 NH1 ARG L 62 75.545 115.348 258.805 1.00 57.15 ATOM 4677 NH2 ARG L 62 75.322 117.628 258.708 1.00 54.05 ATOM 4678 C ARG L 62 78.433 114.690 263.246 1.00 64.06 ATOM 4679 O ARG L 62 78.754 113.525 263.031 1.00 66.59 ATOM 4680 N PHE L 63 79.302 115.698 263.207 1.00 62.89 ATOM 4681 CA PHE L 63 80.727 115.490 262.949 1.00 61.03 ATOM 4682 CB PHE L 63 81.315 116.678 262.174 1.00 60.88 ATOM 4683 CG PHE L 63 80.830 116.780 260.747 1.00 59.48 ATOM 4684 CD1 PHE L 63 79.570 117.289 260.459 1.00 60.59 ATOM 4685 CE1 PHE L 63 79.118 117.383 259.146 1.00 67.90 ATOM 4686 CZ PHE L 63 79.929 116.970 258.102 1.00 54.90 ATOM 4687 CE2 PHE L 63 81.190 116.461 258.376 1.00 66.75 ATOM 4688 CD2 PHE L 63 81.636 116.372 259.695 1.00 67.26 ATOM 4689 C PHE L 63 81.524 115.269 264.235 1.00 64.10 ATOM 4690 O PHE L 63 81.270 115.915 265.264 1.00 63.65 ATOM 4691 N SER L 64 82.486 114.350 264.176 1.00 61.73 ATOM 4692 CA SER L 64 83.412 114.129 265.289 1.00 62.16 ATOM 4693 CB SER L 64 82.789 113.210 266.349 1.00 65.68 ATOM 4694 OG SER L 64 82.431 111.961 265.788 1.00 63.25 ATOM 4695 C SER L 64 84.736 113.554 264.803 1.00 62.26 ATOM 4696 O SER L 64 84.773 112.758 263.865 1.00 67.96 ATOM 4697 N GLY L 65 85.824 113.959 265.447 1.00 60.90 ATOM 4698 CA GLY L 65 87.144 113.440 265.115 1.00 59.43 ATOM 4699 C GLY L 65 87.777 112.737 266.300 1.00 63.62 ATOM 4700 O GLY L 65 87.629 113.166 267.449 1.00 66.33 ATOM 4701 N SER L 66 88.489 111.653 266.027 1.00 62.63 ATOM 4702 CA SER L 66 89.150 110.898 267.080 1.00 64.67 ATOM 4703 CB SER L 66 88.234 109.789 267.597 1.00 68.15 ATOM 4704 OG SER L 66 87.778 108.980 266.527 1.00 70.27 ATOM 4705 C SER L 66 90.460 110.308 266.580 1.00 63.23 ATOM 4706 O SER L 66 90.907 110.614 265.475 1.00 62.59 ATOM 4707 N GLY L 67 91.075 109.468 267.403 1.00 58.52 ATOM 4708 CA GLY L 67 92.326 108.822 267.033 1.00 64.24 ATOM 4709 C GLY L 67 93.515 109.318 267.834 1.00 64.77 ATOM 4710 O GLY L 67 93.374 110.165 268.713 1.00 66.29 ATOM 4711 N SER L 68 94.691 108.782 267.523 1.00 65.75 ATOM 4712 CA SER L 68 95.914 109.138 268.232 1.00 68.10 ATOM 4713 CB SER L 68 95.842 108.677 269.690 1.00 63.62 ATOM 4714 OG SER L 68 95.390 107.338 269.760 1.00 73.26 ATOM 4715 C SER L 68 97.122 108.510 267.560 1.00 67.09 ATOM 4716 O SER L 68 97.012 107.473 266.910 1.00 67.05 ATOM 4717 N GLY L 69 98.276 109.145 267.728 1.00 69.40 ATOM 4718 CA GLY L 69 99.524 108.636 267.184 1.00 65.96 ATOM 4719 C GLY L 69 99.543 108.608 265.670 1.00 67.55 ATOM 4720 O GLY L 69 99.886 109.598 265.020 1.00 68.21 ATOM 4721 N THR L 70 99.140 107.471 265.115 1.00 66.65 ATOM 4722 CA THR L 70 99.283 107.197 263.691 1.00 66.08 ATOM 4723 CB THR L 70 100.084 105.881 263.485 1.00 68.35 ATOM 4724 OG1 THR L 70 101.483 106.183 263.369 1.00 63.80 ATOM 4725 CG2 THR L 70 99.629 105.133 262.250 1.00 74.50 ATOM 4726 C THR L 70 97.942 107.142 262.951 1.00 65.82 ATOM 4727 O THR L 70 97.891 107.320 261.737 1.00 68.08 ATOM 4728 N ASP L 71 96.857 106.916 263.683 1.00 64.98 ATOM 4729 CA ASP L 71 95.556 106.697 263.056 1.00 65.74 ATOM 4730 CB ASP L 71 95.080 105.258 263.288 1.00 68.02 ATOM 4731 CG ASP L 71 96.043 104.229 262.734 1.00 72.59 ATOM 4732 OD1 ASP L 71 96.432 104.347 261.553 1.00 84.90 ATOM 4733 OD2 ASP L 71 96.405 103.294 263.478 1.00 87.07 ATOM 4734 C ASP L 71 94.499 107.670 263.549 1.00 64.28 ATOM 4735 O ASP L 71 94.194 107.720 264.740 1.00 64.38 ATOM 4736 N PHE L 72 93.924 108.424 262.618 1.00 62.71 ATOM 4737 CA PHE L 72 92.917 109.420 262.953 1.00 64.05 ATOM 4738 CB PHE L 72 93.491 110.820 262.760 1.00 63.33 ATOM 4739 CG PHE L 72 94.736 111.055 263.558 1.00 68.77 ATOM 4740 CD1 PHE L 72 94.660 111.379 264.904 1.00 63.13 ATOM 4741 CE1 PHE L 72 95.799 111.576 265.643 1.00 67.10 ATOM 4742 CZ PHE L 72 97.038 111.430 265.054 1.00 66.18 ATOM 4743 CE2 PHE L 72 97.129 111.093 263.722 1.00 60.93 ATOM 4744 CD2 PHE L 72 95.981 110.901 262.982 1.00 61.82 ATOM 4745 C PHE L 72 91.630 109.222 262.160 1.00 65.25 ATOM 4746 O PHE L 72 91.656 108.756 261.017 1.00 63.21 ATOM 4747 N THR L 73 90.505 109.566 262.780 1.00 64.67 ATOM 4748 CA THR L 73 89.201 109.303 262.185 1.00 65.45 ATOM 4749 CB THR L 73 88.512 108.092 262.867 1.00 66.43 ATOM 4750 OG1 THR L 73 89.302 106.916 262.654 1.00 69.67 ATOM 4751 CG2 THR L 73 87.124 107.851 262.284 1.00 68.63 ATOM 4752 C THR L 73 88.275 110.516 262.233 1.00 63.96 ATOM 4753 O THR L 73 88.182 111.206 263.244 1.00 65.15 ATOM 4754 N LEU L 74 87.613 110.779 261.113 1.00 62.20 ATOM 4755 CA LEU L 74 86.497 111.705 261.080 1.00 59.91 ATOM 4756 CB LEU L 74 86.657 112.726 259.950 1.00 58.29 ATOM 4757 CG LEU L 74 85.538 113.766 259.782 1.00 62.55 ATOM 4758 CD1 LEU L 74 85.618 114.835 260.842 1.00 62.02 ATOM 4759 CD2 LEU L 74 85.588 114.422 258.402 1.00 63.84 ATOM 4760 C LEU L 74 85.259 110.860 260.848 1.00 61.09 ATOM 4761 O LEU L 74 85.220 110.038 259.934 1.00 61.83 ATOM 4762 N THR L 75 84.250 111.034 261.683 1.00 61.40 ATOM 4763 CA THR L 75 83.017 110.305 261.474 1.00 65.73 ATOM 4764 CB THR L 75 82.831 109.164 262.523 1.00 65.81 ATOM 4765 OG1 THR L 75 81.439 108.980 262.806 1.00 76.50 ATOM 4766 CG2 THR L 75 83.566 109.473 263.813 1.00 73.89 ATOM 4767 C THR L 75 81.820 111.255 261.398 1.00 63.64 ATOM 4768 O THR L 75 81.824 112.314 262.007 1.00 66.72 ATOM 4769 N ILE L 76 80.828 110.887 260.596 1.00 66.22 ATOM 4770 CA ILE L 76 79.557 111.599 260.552 1.00 63.95 ATOM 4771 CB ILE L 76 79.248 112.139 259.142 1.00 60.81 ATOM 4772 CG1 ILE L 76 80.463 112.853 258.549 1.00 64.35 ATOM 4773 CD1 ILE L 76 80.371 113.084 257.043 1.00 56.75 ATOM 4774 CG2 ILE L 76 78.037 113.062 259.181 1.00 58.10 ATOM 4775 C ILE L 76 78.468 110.603 260.930 1.00 63.02 ATOM 4776 O ILE L 76 78.276 109.618 260.226 1.00 64.30 ATOM 4777 N THR L 77 77.770 110.853 262.038 1.00 65.64 ATOM 4778 CA THR L 77 76.730 109.944 262.535 1.00 63.49 ATOM 4779 CB THR L 77 75.964 110.544 263.733 1.00 64.36 ATOM 4780 OG1 THR L 77 75.610 111.904 263.443 1.00 64.04 ATOM 4781 CG2 THR L 77 76.800 110.488 265.000 1.00 57.96 ATOM 4782 C THR L 77 75.695 109.590 261.474 1.00 66.52 ATOM 4783 O THR L 77 75.362 108.423 261.282 1.00 67.94 ATOM 4784 N ARG L 78 75.168 110.610 260.806 1.00 63.59 ATOM 4785 CA ARG L 78 74.153 110.412 259.783 1.00 66.09 ATOM 4786 CB ARG L 78 72.742 110.497 260.380 1.00 61.94 ATOM 4787 CG ARG L 78 72.572 111.603 261.414 1.00 79.47 ATOM 4788 CD ARG L 78 71.175 111.622 262.034 1.00 77.58 ATOM 4789 NE ARG L 78 70.176 112.196 261.134 1.00 100.30 ATOM 4790 CZ ARG L 78 69.277 111.486 260.457 1.00 106.86 ATOM 4791 NH1 ARG L 78 68.409 112.098 259.661 1.00 106.57 ATOM 4792 NH2 ARG L 78 69.243 110.165 260.576 1.00 111.00 ATOM 4793 C ARG L 78 74.355 111.446 258.688 1.00 63.12 ATOM 4794 O ARG L 78 74.113 112.634 258.888 1.00 62.35 ATOM 4795 N VAL L 79 74.824 110.978 257.538 1.00 61.57 ATOM 4796 CA VAL L 79 75.161 111.846 256.426 1.00 61.58 ATOM 4797 CB VAL L 79 75.770 111.033 255.265 1.00 61.63 ATOM 4798 CG1 VAL L 79 75.702 111.802 253.940 1.00 64.44 ATOM 4799 CG2 VAL L 79 77.199 110.664 255.597 1.00 57.15 ATOM 4800 C VAL L 79 73.945 112.644 255.965 1.00 63.36 ATOM 4801 O VAL L 79 72.823 112.133 255.958 1.00 60.89 ATOM 4802 N GLU L 80 74.176 113.907 255.614 1.00 61.73 ATOM 4803 CA GLU L 80 73.128 114.771 255.077 1.00 63.10 ATOM 4804 CB GLU L 80 72.868 115.954 256.014 1.00 64.69 ATOM 4805 CG GLU L 80 72.336 115.568 257.380 1.00 69.24 ATOM 4806 CD GLU L 80 70.930 115.008 257.320 1.00 82.66 ATOM 4807 OE1 GLU L 80 70.220 115.278 256.328 1.00 90.08 ATOM 4808 OE2 GLU L 80 70.532 114.297 258.268 1.00 88.21 ATOM 4809 C GLU L 80 73.576 115.269 253.709 1.00 62.59 ATOM 4810 O GLU L 80 74.775 115.310 253.437 1.00 62.93 ATOM 4811 N PRO L 81 72.618 115.639 252.839 1.00 61.30 ATOM 4812 CA PRO L 81 72.962 116.025 251.469 1.00 60.48 ATOM 4813 CB PRO L 81 71.636 116.549 250.907 1.00 58.11 ATOM 4814 CG PRO L 81 70.595 115.828 251.691 1.00 57.32 ATOM 4815 CD PRO L 81 71.165 115.700 253.078 1.00 57.39 ATOM 4816 C PRO L 81 74.056 117.091 251.375 1.00 62.56 ATOM 4817 O PRO L 81 74.821 117.095 250.413 1.00 63.73 ATOM 4818 N GLU L 82 74.140 117.980 252.361 1.00 61.94 ATOM 4819 CA GLU L 82 75.147 119.043 252.320 1.00 62.09 ATOM 4820 CB GLU L 82 74.737 120.237 253.194 1.00 63.96 ATOM 4821 CG GLU L 82 74.697 119.952 254.692 1.00 64.98 ATOM 4822 CD GLU L 82 73.342 119.438 255.162 1.00 78.39 ATOM 4823 OE1 GLU L 82 72.576 118.888 254.332 1.00 76.67 ATOM 4824 OE2 GLU L 82 73.043 119.591 256.367 1.00 76.64 ATOM 4825 C GLU L 82 76.546 118.569 252.711 1.00 61.47 ATOM 4826 O GLU L 82 77.500 119.338 252.627 1.00 57.90 ATOM 4827 N ASP L 83 76.666 117.313 253.136 1.00 61.29 ATOM 4828 CA ASP L 83 77.955 116.761 253.551 1.00 62.79 ATOM 4829 CB ASP L 83 77.770 115.588 254.519 1.00 65.92 ATOM 4830 CG ASP L 83 76.972 115.951 255.770 1.00 60.34 ATOM 4831 OD1 ASP L 83 76.905 117.136 256.156 1.00 70.04 ATOM 4832 OD2 ASP L 83 76.417 115.020 256.382 1.00 61.94 ATOM 4833 C ASP L 83 78.772 116.271 252.350 1.00 65.64 ATOM 4834 O ASP L 83 79.971 116.019 252.469 1.00 64.32 ATOM 4835 N PHE L 84 78.120 116.109 251.202 1.00 61.71 ATOM 4836 CA PHE L 84 78.801 115.578 250.023 1.00 65.16 ATOM 4837 CB PHE L 84 77.798 115.183 248.935 1.00 62.96 ATOM 4838 CG PHE L 84 76.897 114.057 249.348 1.00 60.61 ATOM 4839 CD1 PHE L 84 75.531 114.252 249.479 1.00 68.26 ATOM 4840 CE1 PHE L 84 74.701 113.213 249.880 1.00 60.20 ATOM 4841 CZ PHE L 84 75.239 111.966 250.169 1.00 58.91 ATOM 4842 CE2 PHE L 84 76.598 111.762 250.053 1.00 54.96 ATOM 4843 CD2 PHE L 84 77.422 112.809 249.647 1.00 59.19 ATOM 4844 C PHE L 84 79.848 116.557 249.515 1.00 63.32 ATOM 4845 O PHE L 84 79.535 117.688 249.159 1.00 61.71 ATOM 4846 N ALA L 85 81.096 116.108 249.508 1.00 63.54 ATOM 4847 CA ALA L 85 82.225 117.003 249.340 1.00 65.32 ATOM 4848 CB ALA L 85 82.197 118.073 250.430 1.00 59.65 ATOM 4849 C ALA L 85 83.516 116.210 249.435 1.00 64.58 ATOM 4850 O ALA L 85 83.491 114.994 249.627 1.00 65.33 ATOM 4851 N LEU L 86 84.640 116.906 249.306 1.00 64.45 ATOM 4852 CA LEU L 86 85.948 116.316 249.570 1.00 61.92 ATOM 4853 CB LEU L 86 87.018 116.901 248.643 1.00 60.89 ATOM 4854 CG LEU L 86 86.839 116.741 247.128 1.00 69.22 ATOM 4855 CD1 LEU L 86 87.735 117.720 246.373 1.00 74.12 ATOM 4856 CD2 LEU L 86 87.109 115.315 246.692 1.00 67.75 ATOM 4857 C LEU L 86 86.316 116.610 251.012 1.00 62.62 ATOM 4858 O LEU L 86 86.001 117.685 251.526 1.00 62.75 ATOM 4859 N TYR L 87 86.969 115.647 251.657 1.00 60.25 ATOM 4860 CA TYR L 87 87.470 115.806 253.016 1.00 59.93 ATOM 4861 CB TYR L 87 86.700 114.901 253.993 1.00 59.25 ATOM 4862 CG TYR L 87 85.266 115.340 254.150 1.00 63.47 ATOM 4863 CD1 TYR L 87 84.886 116.173 255.193 1.00 58.01 ATOM 4864 CE1 TYR L 87 83.579 116.602 253.325 1.00 66.99 ATOM 4865 CZ TYR L 87 82.635 116.204 254.399 1.00 66.46 ATOM 4866 OH TYR L 87 81.334 116.633 254.521 1.00 56.81 ATOM 4867 CE2 TYR L 87 82.989 115.379 253.352 1.00 66.91 ATOM 4868 CD2 TYR L 87 84.299 114.962 253.224 1.00 60.12 ATOM 4869 C TYR L 87 88.967 115.511 253.055 1.00 61.59 ATOM 4870 O TYR L 87 89.422 114.485 252.538 1.00 63.75 ATOM 4871 N TYR L 88 89.722 116.427 253.654 1.00 62.53 ATOM 4872 CA TYR L 88 91.175 116.304 253.771 1.00 62.80 ATOM 4873 CB TYR L 88 91.851 117.497 253.091 1.00 62.98 ATOM 4874 CG TYR L 88 91.620 117.605 251.602 1.00 63.30 ATOM 4875 CD1 TYR L 88 90.634 118.438 251.086 1.00 60.61 ATOM 4876 CE1 TYR L 88 90.435 118.544 249.717 1.00 57.62 ATOM 4877 CZ TYR L 88 91.226 117.810 248.857 1.00 59.62 ATOM 4878 OH TYR L 88 91.045 117.893 247.498 1.00 65.43 ATOM 4879 CE2 TYR L 88 92.211 116.984 249.349 1.00 60.40 ATOM 4880 CD2 TYR L 88 92.405 116.888 250.709 1.00 60.73 ATOM 4881 C TYR L 88 91.589 116.313 255.232 1.00 63.21 ATOM 4882 O TYR L 88 91.061 117.104 256.003 1.00 64.43 ATOM 4883 N CYS L 89 92.527 115.447 255.617 1.00 67.16 ATOM 4884 CA CYS L 89 93.196 115.590 256.913 1.00 61.76 ATOM 4885 CB CYS L 89 93.499 114.228 257.584 1.00 66.19 ATOM 4886 SG CYS L 89 94.526 113.041 256.646 1.00 71.13 ATOM 4887 C CYS L 89 94.472 116.394 256.695 1.00 64.54 ATOM 4888 O CYS L 89 94.957 116.479 255.564 1.00 62.82 ATOM 4889 N GLN L 90 94.992 117.005 257.762 1.00 62.72 ATOM 4890 CA GLN L 90 96.289 117.684 257.715 1.00 61.37 ATOM 4891 CB GLN L 90 96.158 119.136 257.233 1.00 56.57 ATOM 4892 CG GLN L 90 95.933 120.111 258.364 1.00 67.01 ATOM 4893 CD GLN L 90 96.447 121.507 258.088 1.00 62.12 ATOM 4894 OE1 GLN L 90 96.010 122.460 258.717 1.00 73.22 ATOM 4895 NE2 GLN L 90 97.380 121.634 257.161 1.00 63.55 ATOM 4896 C GLN L 90 96.966 117.697 259.080 1.00 63.70 ATOM 4897 O GLN L 90 96.300 117.718 260.114 1.00 62.39 ATOM 4898 N VAL L 91 98.296 117.689 259.072 1.00 63.89 ATOM 4899 CA VAL L 91 99.075 118.021 260.261 1.00 63.75 ATOM 4900 CB VAL L 91 100.251 117.047 260.459 1.00 62.82 ATOM 4901 CG1 VAL L 91 101.204 117.566 261.527 1.00 65.57 ATOM 4902 CG2 VAL L 91 99.728 115.668 260.841 1.00 66.39 ATOM 4903 C VAL L 91 99.587 119.461 260.134 1.00 61.83 ATOM 4904 O VAL L 91 99.924 119.911 259.039 1.00 65.55 ATOM 4905 N TYR L 92 99.638 120.184 261.247 1.00 60.28 ATOM 4906 CA TYR L 92 100.022 121.595 261.220 1.00 61.98 ATOM 4907 CB TYR L 92 98.776 122.496 261.165 1.00 58.79 ATOM 4908 CG TYR L 92 97.814 122.264 262.305 1.00 55.94 ATOM 4909 CD1 TYR L 92 97.938 122.962 263.503 1.00 60.56 ATOM 4910 CE1 TYR L 92 97.064 122.731 264.560 1.00 65.24 ATOM 4911 CZ TYR L 92 96.054 121.795 264.418 1.00 58.89 ATOM 4912 OH TYR L 92 95.175 121.549 265.452 1.00 60.48 ATOM 4913 CE2 TYR L 92 95.918 121.094 263.241 1.00 58.41 ATOM 4914 CD2 TYR L 92 96.794 121.331 262.193 1.00 60.36 ATOM 4915 C TYR L 92 100.893 121.964 262.415 1.00 61.03 ATOM 4916 O TYR L 92 100.920 121.249 263.415 1.00 64.03 ATOM 4917 N GLY L 93 101.603 123.082 262.299 1.00 63.90 ATOM 4918 CA GLY L 93 102.440 123.597 263.375 1.00 61.34 ATOM 4919 C GLY L 93 103.843 123.019 263.388 1.00 65.84 ATOM 4920 O GLY L 93 104.086 121.933 262.860 1.00 67.80 ATOM 4921 N ALA L 94 104.767 123.751 264.001 1.00 65.72 ATOM 4922 CA ALA L 94 106.155 123.310 264.138 1.00 70.18 ATOM 4923 CB ALA L 94 106.268 122.182 265.169 1.00 67.36 ATOM 4924 C ALA L 94 106.766 122.883 262.808 1.00 70.32 ATOM 4925 O ALA L 94 107.407 121.835 262.718 1.00 72.01 ATOM 4926 N SER L 95 106.550 123.698 261.779 1.00 71.14 ATOM 4927 CA SER L 95 107.176 123.493 260.473 1.00 71.08 ATOM 4928 CB SER L 95 108.698 123.483 260.611 1.00 68.22 ATOM 4929 OG SER L 95 109.137 124.630 261.312 1.00 71.16 ATOM 4930 C SER L 95 106.711 122.225 259.768 1.00 70.32 ATOM 4931 O SER L 95 107.231 121.871 258.712 1.00 72.21 ATOM 4932 N SER L 96 105.736 121.540 260.355 1.00 70.63 ATOM 4933 CA SER L 96 105.194 120.328 259.758 1.00 69.76 ATOM 4934 CB SER L 96 105.182 119.180 260.769 1.00 66.23 ATOM 4935 OG SER L 96 106.489 118.863 261.206 1.00 74.96 ATOM 4936 C SER L 96 103.785 120.580 259.259 1.00 68.90 ATOM 4937 O SER L 96 102.816 120.377 259.988 1.00 76.61 ATOM 4938 N TYR L 97 103.669 121.033 258.019 1.00 65.98 ATOM 4939 CA TYR L 97 102.362 121.211 257.407 1.00 65.25 ATOM 4940 CB TYR L 97 102.172 122.657 256.943 1.00 63.70 ATOM 4941 CG TYR L 97 102.277 123.671 258.061 1.00 57.09 ATOM 4942 CD1 TYR L 97 103.515 124.135 258.486 1.00 54.26 ATOM 4943 CE1 TYR L 97 103.621 125.048 259.514 1.00 51.00 ATOM 4944 CZ TYR L 97 102.480 125.516 260.128 1.00 57.60 ATOM 4945 OH TYR L 97 102.590 126.431 261.146 1.00 62.30 ATOM 4946 CE2 TYR L 97 101.238 125.073 259.726 1.00 54.92 ATOM 4947 CD2 TYR L 97 101.143 124.153 258.697 1.00 56.83 ATOM 4948 C TYR L 97 102.247 120.250 256.239 1.00 66.13 ATOM 4949 O TYR L 97 103.077 120.268 255.333 1.00 72.30 ATOM 4950 N THR L 98 101.227 119.400 256.265 1.00 66.13 ATOM 4951 CA THR L 98 101.083 118.368 255.245 1.00 63.83 ATOM 4952 CB THR L 98 102.086 117.207 255.470 1.00 66.08 ATOM 4953 OG1 THR L 98 102.110 116.348 254.321 1.00 65.22 ATOM 4954 CG2 THR L 98 101.724 116.404 256.713 1.00 55.81 ATOM 4955 C THR L 98 99.646 117.861 255.210 1.00 65.77 ATOM 4956 O THR L 98 98.997 117.745 256.251 1.00 64.64 ATOM 4957 N PHE L 99 99.148 117.587 254.006 1.00 62.29 ATOM 4958 CA PHE L 99 97.751 117.209 253.808 1.00 61.43 ATOM 4959 CB PHE L 99 97.077 118.153 252.811 1.00 59.52 ATOM 4960 CG PHE L 99 96.870 119.557 253.315 1.00 60.36 ATOM 4961 CD1 PHE L 99 97.911 120.478 253.303 1.00 57.92 ATOM 4962 CE1 PHE L 99 97.710 121.778 253.740 1.00 62.83 ATOM 4963 CZ PHE L 99 96.451 122.179 254.174 1.00 58.75 ATOM 4964 CE2 PHE L 99 95.407 121.272 254.182 1.00 62.15 ATOM 4965 CD2 PHE L 99 95.617 119.971 253.748 1.00 53.75 ATOM 4966 C PHE L 99 97.631 115.799 253.244 1.00 59.18 ATOM 4967 O PHE L 99 98.500 115.340 252.507 1.00 53.86 ATOM 4968 N GLY L 100 96.534 115.126 253.576 1.00 61.72 ATOM 4969 CA GLY L 100 96.194 113.853 252.954 1.00 52.85 ATOM 4970 C GLY L 100 95.736 114.120 251.536 1.00 56.53 ATOM 4971 O GLY L 100 95.495 115.273 251.165 1.00 56.19 ATOM 4972 N GLN L 101 95.613 113.067 250.733 1.00 52.32 ATOM 4973 CA GLN L 101 95.225 113.250 249.339 1.00 58.60 ATOM 4974 CB GLN L 101 95.730 112.096 248.457 1.00 54.68 ATOM 4975 CG GLN L 101 94.849 110.862 248.429 1.00 60.79 ATOM 4976 CD GLN L 101 94.957 110.005 249.682 1.00 66.80 ATOM 4977 OE1 GLN L 101 95.531 110.416 250.697 1.00 58.74 ATOM 4978 NE2 GLN L 101 94.395 108.805 249.615 1.00 58.35 ATOM 4979 C GLN L 101 93.713 113.473 249.184 1.00 61.98 ATOM 4980 O GLN L 101 93.221 113.708 248.080 1.00 65.47 ATOM 4981 N GLY L 102 92.984 113.410 250.293 1.00 59.60 ATOM 4982 CA GLY L 102 91.544 113.637 250.259 1.00 61.70 ATOM 4983 C GLY L 102 90.692 112.393 250.083 1.00 62.07 ATOM 4984 O GLY L 102 91.125 111.408 249.493 1.00 59.29 ATOM 4985 N THR L 103 89.478 112.442 250.625 1.00 64.60 ATOM 4986 CA THR L 103 88.477 111.411 250.390 1.00 65.32 ATOM 4987 CB THR L 103 88.122 110.639 251.673 1.00 66.48 ATOM 4988 OG1 THR L 103 89.208 109.782 252.038 1.00 69.47 ATOM 4989 CG2 THR L 103 86.872 109.795 251.456 1.00 61.00 ATOM 4990 C THR L 103 87.208 112.067 249.865 1.00 66.95 ATOM 4991 O THR L 103 86.725 113.042 250.443 1.00 67.95 ATOM 4992 N LYS L 104 86.679 111.539 248.765 1.00 64.55 ATOM 4993 CA LYS L 104 85.424 112.035 248.213 1.00 61.90 ATOM 4994 CB LYS L 104 85.380 111.807 246.704 1.00 58.67 ATOM 4995 CG LYS L 104 84.267 112.557 245.992 1.00 58.23 ATOM 4996 CD LYS L 104 84.184 112.142 244.530 1.00 62.73 ATOM 4997 CE LYS L 104 83.301 113.082 243.740 1.00 74.35 ATOM 4998 NZ LYS L 104 83.167 112.629 242.327 1.00 88.13 ATOM 4999 C LYS L 104 84.220 111.369 248.882 1.00 61.54 ATOM 5000 O LYS L 104 84.093 110.138 248.889 1.00 60.72 ATOM 5001 N LEU L 105 83.351 112.186 249.468 1.00 58.87 ATOM 5002 CA LEU L 105 82.072 111.700 249.958 1.00 60.54 ATOM 5003 CB LEU L 105 81.695 112.394 251.268 1.00 61.67 ATOM 5004 CG LEU L 105 80.790 111.707 252.298 1.00 66.82 ATOM 5005 CD1 LEU L 105 79.945 112.752 253.009 1.00 65.84 ATOM 5006 CD2 LEU L 105 79.905 110.628 251.695 1.00 66.94 ATOM 5007 C LEU L 105 81.027 112.002 248.890 1.00 61.34 ATOM 5008 O LEU L 105 80.544 113.131 248.792 1.00 62.79 ATOM 5009 N GLU L 106 80.694 110.995 248.087 1.00 62.23 ATOM 5010 CA GLU L 106 79.683 111.138 247.047 1.00 61.58 ATOM 5011 CB GLU L 106 80.207 110.627 245.703 1.00 62.07 ATOM 5012 CG GLU L 106 80.751 109.221 245.768 1.00 62.65 ATOM 5013 CD GLU L 106 80.345 108.385 244.577 1.00 69.85 ATOM 5014 OE1 GLU L 106 80.213 107.155 244.735 1.00 73.66 ATOM 5015 OE2 GLU L 106 80.150 108.949 243.483 1.00 73.56 ATOM 5016 C GLU L 106 78.412 110.384 247.430 1.00 61.84 ATOM 5017 O GLU L 106 78.407 109.607 248.372 1.00 63.77 ATOM 5018 N ARG L 107 77.339 110.622 246.684 1.00 61.85 ATOM 5019 CA ARG L 107 76.035 110.066 247.002 1.00 60.71 ATOM 5020 CB ARG L 107 74.937 111.076 246.663 1.00 60.61 ATOM 5021 CG ARG L 107 73.536 110.595 246.966 1.00 62.51 ATOM 5022 CD ARG L 107 72.579 111.763 247.074 1.00 65.60 ATOM 5023 NE ARG L 107 71.210 111.330 247.324 1.00 66.74 ATOM 5024 CZ ARG L 107 70.277 112.092 247.884 1.00 69.00 ATOM 5025 NH1 ARG L 107 70.570 113.330 248.268 1.00 67.91 ATOM 5026 NH2 ARG L 107 69.054 111.615 248.066 1.00 63.60 ATOM 5027 C ARG L 107 75.784 108.745 246.277 1.00 59.20 ATOM 5028 O ARG L 107 75.913 108.655 245.061 1.00 58.49 ATOM 5029 N LYS L 108 75.431 107.722 247.047 1.00 62.03 ATOM 5030 CA LYS L 108 75.153 106.401 246.510 1.00 56.96 ATOM 5031 CB LYS L 108 75.142 105.378 247.645 1.00 57.54 ATOM 5032 CG LYS L 108 74.897 103.936 247.223 1.00 54.84 ATOM 5033 CD LYS L 108 74.978 103.014 248.433 1.00 72.27 ATOM 5034 CE LYS L 108 74.367 101.642 248.149 1.00 88.44 ATOM 5035 NZ LYS L 108 75.066 100.916 247.051 1.00 89.69 ATOM 5036 C LYS L 108 73.814 106.396 245.790 1.00 57.11 ATOM 5037 O LYS L 108 72.870 107.072 246.203 1.00 59.51 ATOM 5038 N ARG L 109 73.752 105.649 244.697 1.00 55.20 ATOM 5039 CA ARG L 109 72.502 105.392 244.000 1.00 54.41 ATOM 5040 CB ARG L 109 72.172 106.522 243.016 1.00 50.62 ATOM 5041 CG ARG L 109 73.110 106.645 241.820 1.00 46.41 ATOM 5042 CD ARG L 109 72.435 106.127 240.561 1.00 56.23 ATOM 5043 NE ARG L 109 71.537 107.130 240.010 1.00 51.45 ATOM 5044 CZ ARG L 109 70.493 106.875 239.233 1.00 52.89 ATOM 5045 NH1 ARG L 109 70.177 105.626 238.902 1.00 44.74 ATOM 5046 NH2 ARG L 109 69.756 107.884 238.792 1.00 62.03 ATOM 5047 C ARG L 109 72.632 104.051 243.294 1.00 55.97 ATOM 5048 O ARG L 109 73.698 103.436 243.326 1.00 56.72 ATOM 5049 N THR L 110 71.550 103.589 242.676 1.00 56.98 ATOM 5050 CA THR L 110 71.587 102.339 241.933 1.00 55.71 ATOM 5051 CB THR L 110 70.180 101.889 241.498 1.00 54.84 ATOM 5052 OG1 THR L 110 69.578 102.908 240.690 1.00 51.25 ATOM 5053 CG2 THR L 110 69.307 101.626 242.713 1.00 52.08 ATOM 5054 C THR L 110 72.478 102.485 240.705 1.00 58.35 ATOM 5055 O THR L 110 72.629 103.577 240.168 1.00 60.31 ATOM 5056 N VAL L 111 73.072 101.377 240.278 1.00 61.43 ATOM 5057 CA VAL L 111 73.960 101.364 239.123 1.00 61.11 ATOM 5058 CB VAL L 111 74.567 99.960 238.906 1.00 61.35 ATOM 5059 CG1 VAL L 111 75.368 99.912 237.618 1.00 62.14 ATOM 5060 CG2 VAL L 111 75.435 99.570 240.093 1.00 55.58 ATOM 5061 C VAL L 111 73.203 101.788 237.877 1.00 61.22 ATOM 5062 O VAL L 111 72.066 101.381 237.664 1.00 63.20 ATOM 5063 N ALA L 112 73.833 102.621 237.061 1.00 64.59 ATOM 5064 CA ALA L 112 73.206 103.100 235.842 1.00 62.53 ATOM 5065 CB ALA L 112 72.711 104.535 236.024 1.00 62.91 ATOM 5066 C ALA L 112 74.190 103.017 234.687 1.00 63.39 ATOM 5067 O ALA L 112 75.264 103.619 234.730 1.00 64.34 ATOM 5068 N ALA L 113 73.822 102.257 233.662 1.00 60.74 ATOM 5069 CA ALA L 113 74.624 102.159 232.456 1.00 58.58 ATOM 5070 CB ALA L 113 74.088 101.053 231.559 1.00 58.73 ATOM 5071 C ALA L 113 74.614 103.492 231.719 1.00 61.20 ATOM 5072 O ALA L 113 73.597 104.187 231.700 1.00 61.97 ATOM 5073 N PRO L 114 75.751 103.859 231.111 1.00 61.37 ATOM 5074 CA PRO L 114 75.807 105.070 230.312 1.00 58.98 ATOM 5075 CB PRO L 114 77.301 105.227 230.031 1.00 59.67 ATOM 5076 CG PRO L 114 77.828 103.849 230.059 1.00 60.46 ATOM 5077 CD PRO L 114 77.040 103.148 231.129 1.00 61.33 ATOM 5078 C PRO L 114 75.074 104.867 228.996 1.00 61.98 ATOM 5079 O PRO L 114 74.981 103.738 228.506 1.00 56.61 ATOM 5080 N SER L 115 74.538 105.951 228.448 1.00 62.99 ATOM 5081 CA SER 5 115 74.072 105.965 227.070 1.00 63.37 ATOM 5082 CB SER L 115 72.881 106.905 226.914 1.00 62.63 ATOM 5083 OG SER L 115 71.708 106.337 227.455 1.00 68.39 ATOM 5084 C SER L 115 75.229 106.469 226.224 1.00 64.73 ATOM 5085 O SER L 115 75.711 107.586 226.428 1.00 66.21 ATOM 5086 N VAL L 116 75.679 105.646 225.284 1.00 62.49 ATOM 5087 CA VAL L 116 76.844 105.989 224.477 1.00 63.79 ATOM 5088 CB VAL L 116 77.778 104.781 224.285 1.00 63.96 ATOM 5089 CG1 VAL L 116 79.040 105.203 223.542 1.00 60.23 ATOM 5090 CG2 VAL L 116 78.129 104.169 225.636 1.00 61.30 ATOM 5091 C VAL L 116 76.472 106.563 223.113 1.00 64.22 ATOM 5092 O VAL L 116 75.684 105.977 222.369 1.00 64.58 ATOM 5093 N PHE L 117 77.054 107.712 222.788 1.00 63.24 ATOM 5094 CA PHE L 117 76.842 108.343 221.494 1.00 59.71 ATOM 5095 CB PHE L 117 75.971 109.593 221.642 1.00 61.88 ATOM 5096 CG PHE L 117 74.721 109.370 222.445 1.00 65.83 ATOM 5097 CD1 PHE L 117 74.690 109.659 223.798 1.00 61.65 ATOM 5098 CE1 PHE L 117 73.543 109.454 224.539 1.00 63.22 ATOM 5099 CZ PHE L 117 72.409 108.953 223.932 1.00 63.85 ATOM 5100 CE2 PHE L 117 72.426 108.659 222.586 1.00 73.61 ATOM 5101 CD2 PHE L 117 73.579 108.867 221.849 1.00 66.50 ATOM 5102 C PHE L 117 78.185 108.727 220.898 1.00 59.26 ATOM 5103 O PHE L 117 79.092 109.154 221.617 1.00 61.29 ATOM 5104 N ILE L 118 78.316 108.574 219.586 1.00 57.81 ATOM 5105 CA ILE L 118 79.544 108.960 218.906 1.00 56.38 ATOM 5106 CB ILE L 118 80.233 107.749 218.224 1.00 59.49 ATOM 5107 CG1 ILE L 118 81.546 108.169 217.554 1.00 56.11 ATOM 5108 CD1 ILE L 118 82.482 107.011 217.279 1.00 61.24 ATOM 5109 CG2 ILE L 118 79.294 107.069 217.226 1.00 56.26 ATOM 5110 C ILE L 118 79.254 110.071 217.904 1.00 56.89 ATOM 5111 O ILE L 118 78.202 110.088 217.264 1.00 58.51 ATOM 5112 N PHE L 119 80.184 111.009 217.786 1.00 58.44 ATOM 5113 CA PHE L 119 80.019 112.135 216.878 1.00 58.01 ATOM 5114 CB PHE L 119 79.876 113.436 217.662 1.00 57.01 ATOM 5115 CG PHE L 119 78.672 113.484 218.551 1.00 53.39 ATOM 5116 CD1 PHE L 119 77.445 113.894 218.055 1.00 54.77 ATOM 5117 CE1 PHE L 119 76.332 113.953 218.878 1.00 58.42 ATOM 5118 CZ PHE L 119 76.440 113.602 220.216 1.00 55.32 ATOM 5119 CE2 PHE L 119 77.659 113.193 220.722 1.00 51.21 ATOM 5120 CD2 PHE L 119 78.769 113.141 219.892 1.00 58.42 ATOM 5121 C PHE L 119 81.196 112.254 215.915 1.00 59.34 ATOM 5122 O PHE L 119 82.333 112.460 216.346 1.00 60.21 ATOM 5123 N PRO L 120 80.923 112.132 214.604 1.00 57.72 ATOM 5124 CA PRO L 120 81.940 112.307 213.570 1.00 56.65 ATOM 5125 CB PRO L 120 81.181 112.007 212.269 1.00 56.00 ATOM 5126 CG PRO L 120 79.952 111.275 212.682 1.00 59.50 ATOM 5127 CD PRO L 120 79.604 111.815 214.033 1.00 57.54 ATOM 5128 C PRO L 120 82.453 113.742 213.545 1.00 56.26 ATOM 5129 O PRO L 120 81.753 114.654 213.996 1.00 58.72 ATOM 5130 N PRO L 121 83.674 113.949 213.027 1.00 57.03 ATOM 5131 CA PRO L 121 84.162 115.313 212.898 1.00 54.97 ATOM 5132 CB PRO L 121 85.595 115.130 212.388 1.00 56.89 ATOM 5133 CG PRO L 121 85.610 113.784 211.745 1.00 53.75 ATOM 5134 CD PRO L 121 84.646 112.954 212.532 1.00 56.06 ATOM 5135 C PRO L 121 83.325 116.054 211.870 1.00 54.90 ATOM 5136 O PRO L 121 83.043 115.518 210.801 1.00 56.08 ATOM 5137 N SER L 122 82.911 117.268 212.205 1.00 56.16 ATOM 5138 CA SER L 122 82.144 118.087 211.283 1.00 58.08 ATOM 5139 CB SER L 122 81.696 119.369 211.978 1.00 58.25 ATOM 5140 OG SER L 122 82.815 120.103 212.445 1.00 64.04 ATOM 5141 C SER L 122 83.005 118.419 210.067 1.00 57.49 ATOM 5142 O SER L 122 84.224 118.557 210.184 1.00 55.91 ATOM 5143 N ASP L 123 82.378 118.533 208.901 1.00 57.61 ATOM 5144 CA ASP L 123 83.124 118.847 207.682 1.00 61.55 ATOM 5145 CB ASP L 123 82.304 118.551 206.414 1.00 64.15 ATOM 5146 CG ASP L 123 80.808 118.703 206.626 1.00 69.06 ATOM 5147 OD1 ASP L 123 80.392 119.049 207.754 1.00 82.22 ATOM 5148 OD2 ASP L 123 80.048 118.470 205.659 1.00 61.81 ATOM 5149 C ASP L 123 83.663 120.277 207.685 1.00 60.05 ATOM 5150 O ASP L 123 84.545 120.618 206.902 1.00 59.81 ATOM 5151 N GLU L 124 83.136 121.107 208.580 1.00 60.99 ATOM 5152 CA GLU L 124 83.688 122.440 208.782 1.00 61.48 ATOM 5153 CB GLU L 124 82.697 123.344 209.527 1.00 62.41 ATOM 5154 CG GLU L 124 81.564 122.594 210.209 1.00 68.53 ATOM 5155 CD GLU L 124 80.356 123.475 210.479 1.00 76.38 ATOM 5156 OE1 GLU L 124 80.517 124.541 211.114 1.00 78.15 ATOM 5157 OE2 GLU L 124 79.242 123.096 210.060 1.00 77.34 ATOM 5158 C GLU L 124 85.044 122.382 209.489 1.00 59.52 ATOM 5159 O GLU L 124 85.952 123.145 209.153 1.00 60.12 ATOM 5160 N GLN L 125 85.190 121.471 210.449 1.00 56.33 ATOM 5161 CA GLN L 125 86.485 121.272 211.099 1.00 54.16 ATOM 5162 CB GLN L 125 86.374 120.424 212.367 1.00 53.45 ATOM 5163 CG GLN L 125 87.714 120.286 213.088 1.00 51.27 ATOM 5164 CD GLN L 125 87.724 119.219 214.165 1.00 55.80 ATOM 5165 OE1 GLN L 125 88.697 119.092 214.909 1.00 51.96 ATOM 5166 NE2 GLN L 125 86.644 118.441 214.252 1.00 57.23 ATOM 5167 C GLN L 125 87.484 120.622 210.154 1.00 53.47 ATOM 5168 O GLN L 125 88.676 120.919 210.207 1.00 51.52 ATOM 5169 N LEU L 126 86.990 119.726 209.302 1.00 53.61 ATOM 5170 CA LEU L 126 87.835 119.041 208.329 1.00 56.96 ATOM 5171 CB LEU L 126 87.028 118.005 207.541 1.00 57.51 ATOM 5172 CG LEU L 126 86.587 116.752 208.304 1.00 56.72 ATOM 5173 CD1 LEU L 126 85.596 115.944 207.478 1.00 58.11 ATOM 5174 CD2 LEU L 126 87.793 115.906 208.683 1.00 55.55 ATOM 5175 C LEU L 126 88.490 120.034 207.379 1.00 57.18 ATOM 5176 O LEU L 126 89.632 119.845 206.964 1.00 57.29 ATOM 5177 N LYS L 127 87.761 121.095 207.045 1.00 58.92 ATOM 5178 CA LYS L 127 88.294 122.148 206.193 1.00 61.50 ATOM 5179 CB LYS L 127 87.229 123.207 205.897 1.00 62.10 ATOM 5180 CG LYS L 127 86.194 122.768 204.865 1.00 66.27 ATOM 5181 CD LYS L 127 85.333 123.935 204.401 1.00 70.53 ATOM 5182 CE LYS L 127 84.319 123.502 203.348 1.00 70.30 ATOM 5183 NZ LYS L 127 84.963 123.066 202.076 1.00 68.38 ATOM 5184 C LYS L 127 89.541 122.781 206.805 1.00 61.17 ATOM 5185 O LYS L 127 90.482 123.116 206.090 1.00 61.32 ATOM 5186 N SER L 128 89.553 122.930 208.127 1.00 61.82 ATOM 5187 CA SER L 128 90.721 123.481 208.816 1.00 62.37 ATOM 5188 CB SER L 128 90.350 124.029 210.202 1.00 63.07 ATOM 5189 OG SER L 128 89.965 122.997 211.096 1.00 62.12 ATOM 5190 C SER L 128 91.857 122.459 208.912 1.00 61.96 ATOM 5191 O SER L 128 92.937 122.760 209.420 1.00 61.83 ATOM 5192 N GLY L 129 91.602 121.250 208.419 1.00 61.50 ATOM 5193 CA GLY L 129 92.633 120.222 208.320 1.00 61.92 ATOM 5194 C GLY L 129 92.805 119.358 209.553 1.00 61.77 ATOM 5195 O GLY L 129 93.823 118.683 209.707 1.00 61.98 ATOM 5196 N THR L 130 91.807 119.374 210.430 1.00 61.84 ATOM 5197 CA THR L 130 91.845 118.599 211.668 1.00 61.85 ATOM 5198 CB THR L 130 92.041 119.515 212.898 1.00 62.05 ATOM 5199 OG1 THR L 130 93.210 120.322 212.713 1.00 68.66 ATOM 5200 CG2 THR L 130 92.199 118.695 214.173 1.00 60.50 ATOM 5201 C THR L 130 90.558 117.796 211.835 1.00 61.38 ATOM 5202 O THR L 130 89.506 118.177 211.314 1.00 60.92 ATOM 5203 N ALA L 131 90.643 116.685 212.560 1.00 58.76 ATOM 5204 CA ALA L 131 89.477 115.849 212.808 1.00 59.28 ATOM 5205 CB ALA L 131 89.476 114.644 211.880 1.00 55.77 ATOM 5206 C ALA L 131 89.401 115.398 214.265 1.00 61.84 ATOM 5207 O ALA L 131 90.255 114.647 214.738 1.00 62.27 ATOM 5208 N SER L 132 88.376 115.868 214.973 1.00 61.34 ATOM 5209 CA SER L 132 88.108 115.407 216.329 1.00 61.91 ATOM 5210 CB SER L 132 87.891 116.589 217.272 1.00 63.40 ATOM 5211 OG SER L 132 89.015 117.453 217.279 1.00 63.74 ATOM 5212 C SER L 132 86.878 114.507 216.332 1.00 62.91 ATOM 5213 O SER L 132 85.848 114.852 215.757 1.00 66.00 ATOM 5214 N VAL L 133 86.993 113.347 216.965 1.00 62.64 ATOM 5215 CA VAL L 133 85.853 112.452 217.115 1.00 62.02 ATOM 5216 CB VAL L 133 86.158 111.016 216.629 1.00 63.53 ATOM 5217 CG1 VAL L 133 84.865 110.221 216.502 1.00 57.61 ATOM 5218 CG2 VAL L 133 86.899 111.039 215.295 1.00 57.00 ATOM 5219 C VAL L 133 85.464 112.417 218.582 1.00 63.50 ATOM 5220 O VAL L 133 86.311 112.208 219.451 1.00 62.54 ATOM 5221 N VAL L 134 84.183 112.634 218.856 1.00 65.74 ATOM 5222 CA VAL L 134 83.712 112.728 220.231 1.00 66.63 ATOM 5223 CB VAL L 134 82.883 114.010 220.466 1.00 66.19 ATOM 5224 CG1 VAL L 134 82.561 114.173 221.947 1.00 64.50 ATOM 5225 CG2 VAL L 134 83.630 115.229 219.949 1.00 62.42 ATOM 5226 C VAL L 134 82.879 111.514 220.609 1.00 67.76 ATOM 5227 O VAL L 134 82.015 111.079 219.850 1.00 69.86 ATOM 5228 N CYS L 135 83.162 110.963 221.784 1.00 69.14 ATOM 5229 CA CYS L 135 82.361 109.885 222.337 1.00 68.40 ATOM 5230 CB CYS L 135 83.213 108.644 222.557 1.00 65.96 ATOM 5231 SG CYS L 135 82.277 107.213 223.118 1.00 74.19 ATOM 5232 C CYS L 135 81.754 110.340 223.660 1.00 68.62 ATOM 5233 O CYS L 135 82.458 110.874 224.515 1.00 67.49 ATOM 5234 N LEU L 136 80.452 110.118 223.822 1.00 67.04 ATOM 5235 CA LEU L 136 79.736 110.581 225.006 1.00 65.14 ATOM 5236 CB LEU L 136 78.630 111.555 224.601 1.00 64.29 ATOM 5237 CG LEU L 136 77.645 111.953 225.699 1.00 66.26 ATOM 5238 CD1 LEU L 136 78.316 112.875 226.718 1.00 61.88 ATOM 5239 CD2 LEU L 136 76.406 112.609 225.101 1.00 59.55 ATOM 5240 C LEU L 136 79.139 109.442 225.829 1.00 64.51 ATOM 5241 O LEU L 136 78.394 108.617 225.309 1.00 65.98 ATOM 5242 N LEU L 137 79.480 109.405 227.115 1.00 63.82 ATOM 5243 CA LEU L 137 78.837 108.504 228.067 1.00 62.75 ATOM 5244 CB LEU L 137 79.871 107.798 228.940 1.00 61.62 ATOM 5245 CG LEU L 137 80.752 106.720 228.313 1.00 61.75 ATOM 5246 CD1 LEU L 137 81.694 107.320 227.274 1.00 62.41 ATOM 5247 CD2 LEU L 137 81.538 106.018 229.406 1.00 60.31 ATOM 5248 C LEU L 137 77.921 109.338 228.945 1.00 61.95 ATOM 5249 O LEU L 137 78.386 110.143 229.742 1.00 61.67 ATOM 5250 N ASN L 138 76.619 109.139 228.800 1.00 60.50 ATOM 5251 CA ASN L 138 75.655 110.012 229.437 1.00 61.87 ATOM 5252 CB ASN L 138 74.617 110.468 228.412 1.00 62.52 ATOM 5253 CG ASN L 138 74.114 111.863 228.683 1.00 67.16 ATOM 5254 OD1 ASN L 138 74.868 112.730 229.121 1.00 75.70 ATOM 5255 ND2 ASN L 138 72.838 112.094 228.415 1.00 69.15 ATOM 5256 C ASN L 138 74.951 109.386 230.640 1.00 63.44 ATOM 5257 O ASN L 138 74.380 108.295 230.533 1.00 60.95 ATOM 5258 N ASN L 139 75.000 110.090 231.774 1.00 61.50 ATOM 5259 CA ASN L 139 74.223 109.744 232.970 1.00 59.15 ATOM 5260 CB ASN L 139 72.736 110.006 232.726 1.00 60.86 ATOM 5261 CG ASN L 139 72.455 111.435 232.307 1.00 62.19 ATOM 5262 OD1 ASN L 139 73.278 112.327 232.506 1.00 72.18 ATOM 5263 ND2 ASN L 139 71.286 111.660 231.723 1.00 65.60 ATOM 5264 C ASN L 139 74.422 108.321 233.495 1.00 62.74 ATOM 5265 O ASN L 139 73.501 107.497 233.464 1.00 63.55 ATOM 5266 N PHE L 140 75.619 108.039 233.994 1.00 61.74 ATOM 5267 CA PHE L 140 75.929 106.717 234.521 1.00 62.95 ATOM 5268 CB PHE L 140 76.990 106.028 233.651 1.00 62.61 ATOM 5269 CG PHE L 140 78.267 106.803 233.525 1.00 55.38 ATOM 5270 CD1 PHE L 140 78.407 107.779 232.549 1.00 63.23 ATOM 5271 CE1 PHE L 140 79.584 108.500 232.431 1.00 56.75 ATOM 5272 CZ PHE L 140 80.639 108.246 233.290 1.00 59.43 ATOM 5273 CE2 PHE L 140 80.515 107.270 234.264 1.00 57.03 ATOM 5274 CD2 PHE L 140 79.332 106.555 234.376 1.00 61.47 ATOM 5275 C PHE L 140 76.387 106.761 235.983 1.00 63.63 ATOM 5276 O PHE L 140 76.774 107.815 236.493 1.00 63.83 ATOM 5277 N TYR L 141 76.329 105.605 236.644 1.00 61.97 ATOM 5278 CA TYR L 141 76.837 105.439 238.001 1.00 58.55 ATOM 5279 CB TYR L 141 75.787 105.858 239.040 1.00 58.80 ATOM 5280 CG TYR L 141 76.318 105.811 240.456 1.00 52.48 ATOM 5281 CD1 TYR L 141 76.198 104.658 241.228 1.00 56.72 ATOM 5282 CE1 TYR L 141 76.706 104.601 242.515 1.00 45.51 ATOM 5283 CZ TYR L 141 77.348 105.702 243.042 1.00 53.78 ATOM 5284 OH TYR L 141 77.852 105.651 244.325 1.00 60.60 ATOM 5285 CE2 TYR L 141 77.486 106.856 242.294 1.00 57.32 ATOM 5286 CD2 TYR L 141 76.976 106.903 241.008 1.00 49.71 ATOM 5287 C TYR L 141 77.228 103.975 238.207 1.00 59.05 ATOM 5288 O TYR L 141 76.482 103.082 237.808 1.00 62.13 ATOM 5289 N PRO L 142 78.386 103.716 238.846 1.00 59.83 ATOM 5290 CA PRO L 142 79.334 104.676 239.424 1.00 62.07 ATOM 5291 CB PRO L 142 80.198 103.802 240.333 1.00 62.33 ATOM 5292 CG PRO L 142 80.178 102.470 239.687 1.00 62.85 ATOM 5293 CD PRO L 142 78.820 102.324 239.062 1.00 58.02 ATOM 5294 C PRO L 142 80.223 105.401 238.415 1.00 62.24 ATOM 5295 O PRO L 142 80.143 105.154 237.214 1.00 61.44 ATOM 5296 N ARG L 143 81.064 106.295 238.927 1.00 63.08 ATOM 5297 CA ARG L 143 81.939 107.121 238.103 1.00 63.69 ATOM 5298 CB ARG L 143 82.703 108.109 238.988 1.00 62.45 ATOM 5299 CG ARG L 143 83.567 109.107 238.237 1.00 64.08 ATOM 5300 CD ARG L 143 84.119 110.160 239.182 1.00 70.86 ATOM 5301 NE ARG L 143 85.269 110.895 238.650 1.00 78.30 ATOM 5302 CZ ARG L 143 85.876 110.636 237.493 1.00 87.04 ATOM 5303 NH1 ARG L 143 86.915 111.369 237.116 1.00 82.44 ATOM 5304 NH2 ARG L 143 85.450 109.651 236.710 1.00 89.67 ATOM 5305 C ARG L 143 82.920 106.290 237.279 1.00 65.62 ATOM 5306 O ARG L 143 83.290 106.680 236.173 1.00 64.85 ATOM 5307 N GLU L 144 83.338 105.150 237.824 1.00 67.35 ATOM 5308 CA GLU L 144 84.293 104.273 237.149 1.00 69.71 ATOM 5309 CB GLU L 144 84.606 103.035 237.998 1.00 71.75 ATOM 5310 CG GLU L 144 85.576 103.283 239.151 1.00 81.96 ATOM 5311 CD GLU L 144 84.972 104.128 240.263 1.00 93.95 ATOM 5312 OE1 GLU L 144 83.811 103.869 240.650 1.00 94.35 ATOM 5313 OE2 GLU L 144 85.663 105.049 240.754 1.00 95.61 ATOM 5314 C GLU L 144 83.788 103.845 235.779 1.00 69.27 ATOM 5315 O GLU L 144 82.762 103.173 235.662 1.00 66.89 ATOM 5316 N ALA L 145 84.518 104.253 234.747 1.00 69.37 ATOM 5317 CA ALA L 145 84.235 103.842 233.379 1.00 70.06 ATOM 5318 CB ALA L 145 83.254 104.798 232.733 1.00 68.26 ATOM 5319 C ALA L 145 85.532 103.797 232.583 1.00 71.11 ATOM 5320 O ALA L 145 86.459 104.560 232.847 1.00 73.56 ATOM 5321 N LYS L 146 85.607 102.893 231.614 1.00 71.23 ATOM 5322 CA LYS L 146 86.755 102.869 230.722 1.00 69.22 ATOM 5323 CB LYS L 146 87.530 101.554 230.843 1.00 69.37 ATOM 5324 CG LYS L 146 88.919 101.605 230.220 1.00 71.74 ATOM 5325 CD LYS L 146 89.773 100.415 230.630 1.00 70.66 ATOM 5326 CE LYS L 146 89.254 99.120 230.035 1.00 66.88 ATOM 5327 NZ LYS L 146 90.125 97.968 230.412 1.00 69.03 ATOM 5328 C LYS L 146 86.322 103.124 229.284 1.00 67.12 ATOM 5329 O LYS L 146 85.360 102.528 228.796 1.00 62.07 ATOM 5330 N VAL L 147 87.034 104.031 228.623 1.00 66.23 ATOM 5331 CA VAL L 147 86.759 104.373 227.236 1.00 66.44 ATOM 5332 CB VAL L 147 86.307 105.840 227.094 1.00 65.63 ATOM 5333 CG1 VAL L 147 85.929 106.137 225.653 1.00 62.06 ATOM 5334 CG2 VAL L 147 85.147 106.134 228.026 1.00 68.97 ATOM 5335 C VAL L 147 88.007 104.179 226.387 1.00 65.07 ATOM 5336 O VAL L 147 89.044 104.791 226.644 1.00 64.41 ATOM 5337 N GLN L 148 87.905 103.324 225.377 1.00 65.08 ATOM 5338 CA GLN L 148 89.017 103.101 224.464 1.00 64.35 ATOM 5339 CB GLN L 148 89.526 101.669 224.573 1.00 64.71 ATOM 5340 CG GLN L 148 90.267 101.385 225.861 1.00 68.69 ATOM 5341 CD GLN L 148 90.877 100.007 225.877 1.00 75.90 ATOM 5342 OE1 GLN L 148 92.085 99.853 226.053 1.00 81.83 ATOM 5343 NE2 GLN L 148 90.046 98.990 225.682 1.00 78.16 ATOM 5344 C GLN L 148 88.615 103.404 223.032 1.00 64.26 ATOM 5345 O GLN L 148 87.491 103.125 222.620 1.00 67.30 ATOM 5346 N TRP L 149 89.539 103.989 222.279 1.00 63.07 ATOM 5347 CA TRP L 149 89.304 104.269 220.874 1.00 63.26 ATOM 5348 CB TRP L 149 89.808 105.667 220.511 1.00 61.29 ATOM 5349 CG TRP L 149 88.951 106.780 221.042 1.00 65.46 ATOM 5350 CD1 TRP L 149 89.126 107.467 222.210 1.00 55.50 ATOM 5351 NE1 TRP L 149 88.144 108.415 222.352 1.00 64.14 ATOM 5352 CE2 TRP L 149 87.307 108.355 221.269 1.00 62.67 ATOM 5353 CD2 TRP L 149 87.785 107.336 220.421 1.00 64.12 ATOM 5354 CE3 TRP L 149 87.100 107.072 219.228 1.00 66.40 ATOM 5355 CZ3 TRP L 149 85.974 107.823 218.928 1.00 64.07 ATOM 5356 CH2 TRP L 149 85.525 108.832 219.793 1.00 60.01 ATOM 5357 CZ2 TRP L 149 86.176 109.111 220.964 1.00 59.11 ATOM 5358 C TRP L 149 89.995 103.214 220.018 1.00 66.17 ATOM 5359 O TRP L 149 91.103 102.777 220.331 1.00 66.76 ATOM 5360 N LYS L 150 89.326 102.791 218.952 1.00 68.27 ATOM 5361 CA LYS L 150 89.913 101.861 217.999 1.00 70.67 ATOM 5362 CB LYS L 150 89.406 100.438 218.238 1.00 72.68 ATOM 5363 CG LYS L 150 89.960 99.803 219.504 1.00 75.44 ATOM 5364 CD LYS L 150 89.352 98.441 219.777 1.00 76.74 ATOM 5365 CE LYS L 150 89.900 97.858 221.070 1.00 74.80 ATOM 5366 NZ LYS L 150 89.297 96.535 221.385 1.00 71.92 ATOM 5367 C LYS L 150 89.611 102.317 216.581 1.00 71.58 ATOM 5368 O LYS L 150 88.461 102.591 216.237 1.00 72.49 ATOM 5369 N VAL L 151 90.657 102.420 215.768 1.00 71.61 ATOM 5370 CA VAL L 151 90.516 102.867 214.390 1.00 71.02 ATOM 5371 CB VAL L 151 91.340 104.134 214.115 1.00 71.35 ATOM 5372 CG1 VAL L 151 91.242 104.515 212.653 1.00 67.75 ATOM 5373 CG2 VAL L 151 90.867 105.279 215.001 1.00 64.66 ATOM 5374 C VAL L 151 90.946 101.758 213.446 1.00 73.50 ATOM 5375 O VAL L 151 92.129 101.414 213.364 1.00 73.69 ATOM 5376 N ASP L 152 89.972 101.202 212.735 1.00 77.06 ATOM 5377 CA ASP L 152 90.181 100.000 211.945 1.00 75.82 ATOM 5378 CB ASP L 152 91.095 100.282 210.752 1.00 81.55 ATOM 5379 CG ASP L 152 90.452 101.269 209.759 1.00 82.08 ATOM 5380 OD1 ASP L 152 89.102 101.186 209.680 1.00 77.75 ATOM 5381 OD2 ASP L 152 91.280 101.962 209.065 1.00 83.99 ATOM 5382 C ASP L 152 90.723 98.873 212.824 1.00 75.63 ATOM 5383 O ASP L 152 91.639 98.142 212.435 1.00 74.92 ATOM 5384 N ASN L 153 90.140 98.754 214.016 1.00 72.05 ATOM 5385 CA ASN L 153 90.450 97.679 214.963 1.00 71.65 ATOM 5386 CB ASN L 153 90.397 96.309 214.278 1.00 67.61 ATOM 5387 CG ASN L 153 88.987 95.892 213.909 1.00 65.91 ATOM 5388 OD1 ASN L 153 88.789 95.041 213.040 1.00 85.63 ATOM 5389 ND2 ASN L 153 88.000 96.481 214.570 1.00 60.04 ATOM 5390 C ASN L 153 91.773 97.838 215.712 1.00 70.85 ATOM 5391 O ASN L 153 92.171 96.954 216.474 1.00 71.67 ATOM 5392 N ALA L 154 92.450 98.962 215.493 1.00 68.00 ATOM 5393 CA ALA L 154 93.706 99.236 216.178 1.00 65.68 ATOM 5394 CB ALA L 154 94.713 99.858 215.218 1.00 63.09 ATOM 5395 C ALA L 154 93.471 100.149 217.378 1.00 64.74 ATOM 5396 O ALA L 154 92.804 101.176 217.265 1.00 65.15 ATOM 5397 N LEU L 155 94.018 99.763 218.527 1.00 64.44 ATOM 5398 CA LEU L 155 93.888 100.552 219.746 1.00 65.36 ATOM 5399 CB LEU L 155 94.319 99.732 220.967 1.00 65.15 ATOM 5400 CG LEU L 155 94.223 100.445 222.322 1.00 68.49 ATOM 5401 CD1 LEU L 155 92.796 100.888 222.609 1.00 68.17 ATOM 5402 CD2 LEU L 155 94.746 99.559 223.444 1.00 66.35 ATOM 5403 C LEU L 155 94.698 101.847 219.670 1.00 65.26 ATOM 5404 O LEU L 155 95.919 101.819 219.506 1.00 64.35 ATOM 5405 N GLN L 156 94.009 102.978 219.793 1.00 64.55 ATOM 5406 CA GLN L 156 94.659 104.286 219.751 1.00 65.27 ATOM 5407 CB GLN L 156 93.669 105.364 219.304 1.00 65.47 ATOM 5408 CG GLN L 156 93.129 105.167 217.893 1.00 67.01 ATOM 5409 CD GLN L 156 94.216 105.211 216.833 1.00 72.27 ATOM 5410 OE1 GLN L 156 95.034 106.131 216.801 1.00 73.12 ATOM 5411 NE2 GLN L 156 94.226 104.214 215.954 1.00 71.61 ATOM 5412 C GLN L 156 95.266 104.649 221.104 1.00 64.96 ATOM 5413 O GLN L 156 94.737 104.278 222.151 1.00 62.67 ATOM 5414 N SER L 157 96.382 105.374 221.074 1.00 66.80 ATOM 5415 CA SER L 157 97.093 105.748 222.295 1.00 68.21 ATOM 5416 CB SER L 157 98.164 104.708 222.632 1.00 68.22 ATOM 5417 OG SER L 157 97.577 103.473 222.998 1.00 72.52 ATOM 5418 C SER L 157 97.733 107.129 222.197 1.00 68.02 ATOM 5419 O SER L 157 98.422 107.437 221.221 1.00 67.88 ATOM 5420 N GLY L 158 97.501 107.955 223.215 1.00 67.05 ATOM 5421 CA GLY L 158 98.133 109.268 223.306 1.00 66.55 ATOM 5422 C GLY L 158 97.620 110.272 222.293 1.00 65.19 ATOM 5423 O GLY L 158 98.350 111.171 221.870 1.00 65.54 ATOM 5424 N ASN L 159 96.362 110.112 221.896 1.00 61.30 ATOM 5425 CA ASN L 159 95.726 111.037 220.965 1.00 58.54 ATOM 5426 CB ASN L 159 95.802 110.512 219.530 1.00 56.29 ATOM 5427 CG ASN L 159 95.412 109.050 219.415 1.00 56.35 ATOM 5428 OD1 ASN L 159 94.786 108.482 220.312 1.00 51.58 ATOM 5429 ND2 ASN L 159 95.783 108.432 218.300 1.00 40.89 ATOM 5430 C ASN L 159 94.282 111.317 221.354 1.00 59.19 ATOM 5431 O ASN L 159 93.498 111.832 220.557 1.00 59.79 ATOM 5432 N SER L 160 93.935 110.968 222.587 1.00 59.38 ATOM 5433 CA SER L 160 92.607 111.250 223.102 1.00 62.09 ATOM 5434 CB SER L 160 91.716 110.006 223.037 1.00 61.22 ATOM 5435 OG SER L 160 92.079 109.060 224.026 1.00 63.96 ATOM 5436 C SER L 160 92.683 111.776 224.529 1.00 63.44 ATOM 5437 O SER L 160 93.624 111.475 225.268 1.00 64.04 ATOM 5438 N GLN L 161 91.693 112.580 224.897 1.00 62.63 ATOM 5439 CA GLN L 161 91.548 113.055 226.262 1.00 62.83 ATOM 5440 CB GLN L 161 91.962 114.516 226.373 1.00 63.03 ATOM 5441 CG GLN L 161 93.456 114.734 226.396 1.00 64.25 ATOM 5442 CD GLN L 161 93.820 116.192 226.251 1.00 71.55 ATOM 5443 OE1 GLN L 161 93.438 116.843 225.277 1.00 75.11 ATOM 5444 NE2 GLN L 161 94.561 116.718 227.221 1.00 66.80 ATOM 5445 C GLN L 161 90.097 112.908 226.654 1.00 61.68 ATOM 5446 O GLN L 161 89.220 112.874 225.795 1.00 65.54 ATOM 5447 N GLU L 162 89.838 112.815 227.950 1.00 61.28 ATOM 5448 CA GLU L 162 88.465 112.717 228.414 1.00 61.04 ATOM 5449 CB GLU L 162 88.131 111.285 228.838 1.00 61.71 ATOM 5450 CG GLU L 162 88.737 110.850 230.155 1.00 64.34 ATOM 5451 CD GLU L 162 88.596 109.357 230.370 1.00 65.88 ATOM 5452 OE1 GLU L 162 88.450 108.924 231.534 1.00 71.70 ATOM 5453 OE2 GLU L 162 88.623 108.614 229.368 1.00 66.20 ATOM 5454 C GLU L 162 88.171 113.705 229.535 1.00 58.57 ATOM 5455 O GLU L 162 89.086 114.265 230.136 1.00 55.12 ATOM 5456 N SER L 163 86.883 113.914 229.797 1.00 56.97 ATOM 5457 CA SER L 163 86.432 114.856 230.810 1.00 58.17 ATOM 5458 CB SER L 163 86.177 116.234 230.194 1.00 55.02 ATOM 5459 OG SER L 163 85.677 117.141 231.162 1.00 59.74 ATOM 5460 C SER L 163 85.160 114.331 231.461 1.00 59.12 ATOM 5461 O SER L 163 84.304 113.748 230.792 1.00 57.59 ATOM 5462 N VAL L 164 85.045 114.542 232.769 1.00 60.09 ATOM 5463 CA VAL L 164 83.916 114.029 233.532 1.00 59.86 ATOM 5464 CB VAL L 164 84.357 112.918 234.511 1.00 62.08 ATOM 5465 CG1 VAL L 164 83.147 112.103 234.986 1.00 54.46 ATOM 5466 CG2 VAL L 164 85.376 112.011 233.846 1.00 63.76 ATOM 5467 C VAL L 164 83.232 115.146 234.310 1.00 59.79 ATOM 5468 O VAL L 164 83.892 115.993 234.913 1.00 59.45 ATOM 5469 N THR L 165 81.905 115.145 234.291 1.00 58.67 ATOM 5470 CA THR L 165 81.132 116.142 235.018 1.00 59.95 ATOM 5471 CB THR L 165 79.662 116.168 234.534 1.00 63.45 ATOM 5472 OG1 THR L 165 79.040 114.902 234.800 1.00 63.04 ATOM 5473 CG2 THR L 165 79.590 116.461 233.031 1.00 58.37 ATOM 5474 C THR L 165 81.164 115.860 236.519 1.00 60.65 ATOM 5475 O THR L 165 81.526 114.765 236.939 1.00 57.82 ATOM 5476 N GLU L 166 80.808 116.858 237.324 1.00 63.07 ATOM 5477 CA GLU L 166 80.592 116.642 238.747 1.00 62.41 ATOM 5478 CB GLU L 166 80.481 117.967 239.502 1.00 63.92 ATOM 5479 CG GLU L 166 81.798 118.723 239.647 1.00 74.74 ATOM 5480 CD GLU L 166 82.854 117.921 240.388 1.00 84.60 ATOM 5481 OE1 GLU L 166 82.722 127.756 241.619 1.00 83.50 ATOM 5482 OE2 GLU L 166 83.818 117.460 239.739 1.00 91.53 ATOM 5483 C GLU L 166 79.300 115.851 238.893 1.00 62.35 ATOM 5484 O GLU L 166 78.450 115.874 237.999 1.00 60.03 ATOM 5485 N GLN L 167 79.153 115.155 240.014 1.00 58.32 ATOM 5486 CA GLN L 167 77.973 114.323 240.234 1.00 60.94 ATOM 5487 CB GLN L 167 78.040 113.624 241.595 1.00 56.79 ATOM 5488 CG GLN L 167 76.880 112.675 241.828 1.00 57.66 ATOM 5489 CD GLN L 167 77.059 111.813 243.053 1.00 52.24 ATOM 5490 OE1 GLN L 167 77.541 112.274 244.090 1.00 54.74 ATOM 5491 NE2 GLN L 167 76.663 110.547 242.945 1.00 59.63 ATOM 5492 C GLN L 167 76.699 115.151 240.140 1.00 58.70 ATOM 5493 O GLN L 167 76.538 116.136 240.852 1.00 55.91 ATOM 5494 N ASP L 168 75.787 114.745 239.266 1.00 61.92 ATOM 5495 CA ASP L 168 74.541 115.481 239.099 1.00 62.39 ATOM 5496 CB ASP L 168 73.688 114.851 237.999 1.00 61.47 ATOM 5497 CG ASP L 168 72.516 115.723 237.605 1.00 66.40 ATOM 5498 OD1 ASP L 168 72.702 116.630 236.768 1.00 68.00 ATOM 5499 OD2 ASP L 168 71.407 115.500 238.131 1.00 70.24 ATOM 5500 C ASP L 168 73.763 115.547 240.417 1.00 64.49 ATOM 5501 O ASP L 168 73.600 114.541 241.106 1.00 64.64 ATOM 5502 N SER L 169 73.286 116.738 240.761 1.00 62.63 ATOM 5503 CA SER L 169 72.583 116.950 242.024 1.00 65.92 ATOM 5504 CB SER L 169 72.564 118.439 242.372 1.00 66.91 ATOM 5505 OG SER L 169 71.748 119.155 241.456 1.00 69.60 ATOM 5506 C SER L 169 71.148 116.435 242.016 1.00 67.44 ATOM 5507 O SER L 169 70.477 116.454 243.048 1.00 69.10 ATOM 5508 N LYS L 170 70.669 115.992 240.857 1.00 68.12 ATOM 5509 CA LYS L 170 69.283 115.531 240.736 1.00 65.95 ATOM 5510 CB LYS L 170 68.596 116.180 239.530 1.00 67.41 ATOM 5511 CG LYS L 170 67.873 117.489 239.836 1.00 72.80 ATOM 5512 CD LYS L 170 68.692 118.394 240.739 1.00 77.33 ATOM 5513 CE LYS L 170 67.983 119.710 241.001 1.00 74.83 ATOM 5514 NZ LYS L 170 67.917 120.540 239.770 1.00 70.54 ATOM 5515 C LYS L 170 69.188 114.012 240.644 1.00 65.77 ATOM 5516 O LYS L 170 68.430 113.386 241.385 1.00 67.96 ATOM 5517 N ASP L 171 69.950 113.418 239.730 1.00 64.68 ATOM 5518 CA ASP L 171 69.937 111.967 239.584 1.00 65.70 ATOM 5519 CB ASP L 171 69.656 111.550 238.131 1.00 68.39 ATOM 5520 CG ASP L 171 70.685 112.085 237.145 1.00 72.68 ATOM 5521 OD1 ASP L 171 70.303 112.381 235.993 1.00 80.13 ATOM 5522 OD2 ASP L 171 71.873 112.203 237.510 1.00 74.82 ATOM 5523 C ASP L 171 71.218 111.326 240.110 1.00 63.51 ATOM 5524 O ASP L 171 71.356 110.108 240.090 1.00 63.37 ATOM 5525 N SER L 172 72.150 112.152 240.576 1.00 59.31 ATOM 5526 CA SER L 172 73.391 111.657 241.163 1.00 57.50 ATOM 5527 CB SER L 172 73.095 110.817 242.410 1.00 60.52 ATOM 5528 OG SER L 172 72.251 111.515 243.305 1.00 59.20 ATOM 5529 C SER L 172 74.241 110.845 240.188 1.00 56.60 ATOM 5530 O SER L 172 75.051 110.018 240.608 1.00 54.05 ATOM 5531 N THR L 173 74.053 111.072 238.891 1.00 58.43 ATOM 5532 CA THR L 173 74.828 110.365 237.874 1.00 55.59 ATOM 5533 CB THR L 173 73.952 109.949 236.665 1.00 61.16 ATOM 5534 OG1 THR L 173 73.383 111.116 236.053 1.00 66.92 ATOM 5535 CG2 THR L 173 72.831 109.006 237.090 1.00 52.23 ATOM 5536 C THR L 173 75.999 111.213 237.371 1.00 58.13 ATOM 5537 O THR L 173 76.082 112.412 237.656 1.00 58.32 ATOM 5538 N TYR L 174 76.902 110.577 236.628 1.00 58.70 ATOM 5539 CA TYR L 174 78.008 111.268 235.980 1.00 57.28 ATOM 5540 CB TYR L 174 79.346 110.628 236.358 1.00 56.75 ATOM 5541 CG TYR L 174 79.684 110.746 237.825 1.00 60.59 ATOM 5542 CD1 TYR L 174 79.247 109.791 238.737 1.00 61.86 ATOM 5543 CE1 TYR L 174 79.548 109.896 240.080 1.00 62.78 ATOM 5544 CZ TYR L 174 80.293 110.966 240.526 1.00 60.97 ATOM 5545 OH TYR L 174 80.594 111.072 241.861 1.00 61.76 ATOM 5546 CE2 TYR L 174 80.741 111.929 239.641 1.00 62.02 ATOM 5547 CD2 TYR L 174 80.435 111.813 238.301 1.00 57.91 ATOM 5548 C TYR L 174 77.842 111.202 234.472 1.00 60.02 ATOM 5549 O TYR L 174 77.156 110.324 233.951 1.00 58.74 ATOM 5550 N SER L 175 78.472 112.136 233.773 1.00 61.97 ATOM 5551 CA SER L 175 78.591 112.041 232.325 1.00 61.77 ATOM 5552 CB SER L 175 77.686 113.054 231.629 1.00 60.78 ATOM 5553 OG SER L 175 76.326 112.723 231.832 1.00 62.94 ATOM 5554 C SER L 175 80.048 112.243 231.931 1.00 61.52 ATOM 5555 O SER L 175 80.791 112.943 232.620 1.00 64.11 ATOM 5556 N LEU L 176 80.455 111.619 230.832 1.00 58.82 ATOM 5557 CA LEU L 176 81.845 111.648 230.420 1.00 61.67 ATOM 5558 CB LEU L 176 82.557 110.369 230.881 1.00 61.54 ATOM 5559 CG LEU L 176 84.032 110.147 230.523 1.00 62.26 ATOM 5560 CD1 LEU L 176 84.681 109.197 231.516 1.00 63.54 ATOM 5561 CD2 LEU L 176 84.198 109.622 229.098 1.00 56.46 ATOM 5562 C LEU L 176 81.969 111.807 228.914 1.00 63.36 ATOM 5563 O LEU L 176 81.236 111.185 228.145 1.00 62.95 ATOM 5564 N SER L 177 82.906 112.648 228.496 1.00 65.50 ATOM 5565 CA SER L 177 83.243 112.752 227.089 1.00 65.96 ATOM 5566 CB SER L 177 83.094 114.185 226.609 1.00 62.89 ATOM 5567 OG SER L 177 84.251 114.926 226.947 1.00 75.81 ATOM 5568 C SER L 177 84.682 112.315 226.897 1.00 66.60 ATOM 5569 O SER L 177 85.528 112.552 227.756 1.00 68.08 ATOM 5570 N SER L 178 84.950 111.660 225.775 1.00 67.53 ATOM 5571 CA SER L 178 86.313 111.345 225.377 1.00 67.30 ATOM 5572 CB SER L 178 86.564 109.841 225.447 1.00 69.20 ATOM 5573 OG SER L 178 87.862 109.519 224.977 1.00 72.97 ATOM 5574 C SER L 178 86.501 111.847 223.956 1.00 65.75 ATOM 5575 O SER L 178 85.699 111.536 223.077 1.00 69.39 ATOM 5576 N THR L 179 87.541 112.643 223.740 1.00 62.56 ATOM 5577 CA THR L 179 87.781 113.239 222.436 1.00 63.37 ATOM 5578 CB THR L 179 87.944 114.769 222.529 1.00 66.51 ATOM 5579 OG1 THR L 179 86.831 115.333 223.235 1.00 74.86 ATOM 5580 CG2 THR L 179 88.029 115.385 221.133 1.00 61.43 ATOM 5581 C THR L 179 89.031 112.655 221.793 1.00 64.76 ATOM 5582 O THR L 179 90.127 112.758 222.342 1.00 66.15 ATOM 5583 N LEU L 180 88.848 112.041 220.628 1.00 62.68 ATOM 5584 CA LEU L 180 89.946 111.501 219.835 1.00 62.35 ATOM 5585 CB LEU L 180 89.495 110.202 219.162 1.00 61.00 ATOM 5586 CG LEU L 180 90.452 109.256 218.424 1.00 66.87 ATOM 5587 CD1 LEU L 180 90.460 109.535 216.931 1.00 70.71 ATOM 5588 CD2 LEU L 180 91.862 109.276 219.006 1.00 67.55 ATOM 5589 C LEU L 180 90.326 112.546 218.795 1.00 60.34 ATOM 5590 O LEU L 180 89.475 113.008 218.038 1.00 61.69 ATOM 5591 N THR L 181 91.595 112.940 218.766 1.00 59.13 ATOM 5592 CA THR L 181 92.022 114.004 217.862 1.00 58.98 ATOM 5593 CB THR L 181 92.500 115.246 218.632 1.00 58.03 ATOM 5594 OG1 THR L 181 91.461 115.685 219.516 1.00 63.49 ATOM 5595 CG2 THR L 181 92.850 116.369 217.666 1.00 49.66 ATOM 5596 C THR L 181 93.114 113.557 216.899 1.00 61.94 ATOM 5597 O THR L 181 94.209 113.170 217.312 1.00 64.08 ATOM 5598 N LEU L 182 92.805 113.623 215.610 1.00 62.80 ATOM 5599 CA LEU L 182 93.748 113.239 214.578 1.00 61.72 ATOM 5600 CB LEU L 182 93.278 111.963 213.876 1.00 65.68 ATOM 5601 CG LEU L 182 92.983 110.738 214.742 1.00 65.77 ATOM 5602 CD1 LEU L 182 92.542 109.580 213.864 1.00 69.40 ATOM 5603 CD2 LEU L 182 94.195 110.352 215.579 1.00 69.36 ATOM 5604 C LEU L 182 93.903 114.351 213.552 1.00 62.60 ATOM 5605 O LEU L 182 93.116 115.298 213.522 1.00 61.52 ATOM 5606 N SER L 183 94.928 114.229 212.714 1.00 61.06 ATOM 5607 CA SER L 183 95.103 115.129 211.589 1.00 59.38 ATOM 5608 CB SER L 183 96.548 115.080 211.097 1.00 61.09 ATOM 5609 OG SER L 183 96.885 113.777 210.647 1.00 61.36 ATOM 5610 C SER L 183 94.156 114.700 210.475 1.00 59.62 ATOM 5611 O SER L 183 93.730 113.546 210.429 1.00 58.79 ATOM 5612 N LYS L 184 93.820 115.631 209.588 1.00 60.37 ATOM 5613 CA LYS L 184 92.985 115.321 208.433 1.00 63.32 ATOM 5614 CB LYS L 184 92.842 116.552 207.534 1.00 65.46 ATOM 5615 CG LYS L 184 91.969 116.352 206.302 1.00 68.43 ATOM 5616 CD LYS L 184 92.130 117.512 205.325 1.00 70.15 ATOM 5617 CE LYS L 184 91.138 117.414 204.177 1.00 71.38 ATOM 5618 NZ LYS L 184 89.729 117.461 204.663 1.00 73.41 ATOM 5619 C LYS L 184 93.593 114.167 207.644 1.00 64.09 ATOM 5620 O LYS L 184 92.878 113.292 207.160 1.00 63.41 ATOM 5621 N ALA L 185 94.918 114.173 207.528 1.00 64.20 ATOM 5622 CA ALA L 185 95.641 113.132 206.809 1.00 64.50 ATOM 5623 CB ALA L 185 97.124 113.473 206.732 1.00 63.65 ATOM 5624 C ALA L 185 95.437 111.755 207.441 1.00 64.09 ATOM 5625 O ALA L 185 95.035 110.810 206.762 1.00 63.87 ATOM 5626 N ASP L 186 95.710 111.648 208.740 1.00 63.12 ATOM 5627 CA ASP L 186 95.547 110.386 209.461 1.00 61.99 ATOM 5628 CB ASP L 186 96.065 110.506 210.896 1.00 61.76 ATOM 5629 CG ASP L 186 97.577 110.607 210.968 1.00 65.37 ATOM 5630 OD1 ASP L 186 98.206 110.969 209.947 1.00 63.22 ATOM 5631 OD2 ASP L 186 98.137 110.324 212.051 1.00 66.42 ATOM 5632 C ASP L 186 94.092 109.941 209.482 1.00 59.64 ATOM 5633 O ASP L 186 93.796 108.754 209.618 1.00 60.10 ATOM 5634 N TYR L 187 93.186 110.904 209.351 1.00 57.95 ATOM 5635 CA TYR L 187 91.760 110.618 209.372 1.00 55.99 ATOM 5636 CB TYR L 187 90.956 111.888 209.676 1.00 51.35 ATOM 5637 CG TYR L 187 89.459 111.667 209.704 1.00 52.22 ATOM 5638 CD1 TYR L 187 88.872 110.842 210.667 1.00 46.05 ATOM 5639 CE1 TYR L 187 87.501 110.635 210.695 1.00 46.97 ATOM 5640 CZ TYR L 187 86.703 111.263 209.755 1.00 46.02 ATOM 5641 OH TYR L 187 85.341 111.070 209.762 1.00 47.37 ATOM 5642 CE2 TYR L 187 87.264 112.090 208.793 1.00 50.40 ATOM 5643 CD2 TYR L 187 88.632 112.285 208.770 1.00 57.94 ATOM 5644 C TYR L 187 91.292 109.981 208.065 1.00 57.76 ATOM 5645 O TYR L 187 90.488 109.047 208.079 1.00 57.42 ATOM 5646 N GLU L 188 91.801 110.487 206.943 1.00 60.62 ATOM 5647 CA GLU L 188 91.419 109.976 205.629 1.00 63.40 ATOM 5648 CB GLU L 188 92.117 110.756 204.508 1.00 64.43 ATOM 5649 CG GLU L 188 91.937 112.269 204.554 1.00 68.91 ATOM 5650 CD GLU L 188 90.512 112.716 204.275 1.00 73.19 ATOM 5651 OE1 GLU L 188 89.573 112.151 204.875 1.00 74.17 ATOM 5652 OE2 GLU L 188 90.333 113.647 203.461 1.00 74.21 ATOM 5653 C GLU L 188 91.741 108.494 205.492 1.00 63.86 ATOM 5654 O GLU L 188 90.879 107.698 205.127 1.00 65.94 ATOM 5655 N LYS L 189 92.983 108.133 205.803 1.00 64.52 ATOM 5656 CA LYS L 189 93.492 106.780 205.559 1.00 65.90 ATOM 5657 CB LYS L 189 95.015 106.741 205.737 1.00 66.86 ATOM 5658 CG LYS L 189 95.534 107.607 206.875 1.00 66.53 ATOM 5659 CD LYS L 189 97.050 107.758 206.814 1.00 65.02 ATOM 5660 CE LYS L 189 97.755 106.509 207.319 1.00 68.07 ATOM 5661 NZ LYS L 189 97.432 106.230 208.748 1.00 70.44 ATOM 5662 C LYS L 189 92.823 105.675 206.383 1.00 65.27 ATOM 5663 O LYS L 189 93.257 104.522 206.351 1.00 64.56 ATOM 5664 N HIS L 190 91.769 106.028 207.113 1.00 63.99 ATOM 5665 CA HIS L 190 90.981 105.045 207.852 1.00 63.11 ATOM 5666 CB HIS L 190 91.290 105.118 209.347 1.00 63.76 ATOM 5667 CG HIS L 190 92.743 104.966 209.674 1.00 69.04 ATOM 5668 ND1 HIS L 190 93.487 105.977 210.243 1.00 76.96 ATOM 5669 CE1 HIS L 190 94.729 105.562 210.420 1.00 78.33 ATOM 5670 NE2 HIS L 190 94.818 104.319 209.984 1.00 79.36 ATOM 5671 CD2 HIS L 190 93.590 103.922 209.514 1.00 76.26 ATOM 5672 C HIS L 190 89.491 105.271 207.610 1.00 60.54 ATOM 5673 O HIS L 190 89.090 106.354 207.181 1.00 59.18 ATOM 5674 N LYS L 191 88.670 104.258 207.880 1.00 58.15 ATOM 5675 CA LYS L 191 87.228 104.393 207.663 1.00 59.34 ATOM 5676 CB LYS L 191 86.772 103.609 206.426 1.00 59.24 ATOM 5677 CG LYS L 191 86.682 102.107 206.619 1.00 63.81 ATOM 5678 CD LYS L 191 85.971 101.441 205.449 1.00 66.47 ATOM 5679 CE LYS L 191 84.537 101.932 205.324 1.00 66.79 ATOM 5680 NZ LYS L 191 83.756 101.116 204.355 1.00 68.24 ATOM 5681 C LYS L 191 86.356 104.043 208.876 1.00 58.70 ATOM 5682 O LYS L 191 85.363 104.723 209.139 1.00 56.35 ATOM 5683 N VAL L 192 86.716 102.989 209.605 1.00 59.41 ATOM 5684 CA VAL L 192 85.941 102.588 210.783 1.00 58.53 ATOM 5685 CB VAL L 192 85.908 101.058 210.974 1.00 60.58 ATOM 5686 CG1 VAL L 192 85.144 100.704 212.250 1.00 53.56 ATOM 5687 CG2 VAL L 192 85.286 100.376 209.758 1.00 58.64 ATOM 5688 C VAL L 192 86.473 103.228 212.060 1.00 58.97 ATOM 5689 O VAL L 192 87.600 102.956 212.484 1.00 57.39 ATOM 5690 N TYR L 193 85.647 104.078 212.664 1.00 57.87 ATOM 5691 CA TYR L 193 86.001 104.760 213.903 1.00 58.17 ATOM 5692 CB TYR L 193 85.984 106.278 213.702 1.00 55.96 ATOM 5693 CG TYR L 193 87.121 106.748 212.828 1.00 58.29 ATOM 5694 CD1 TYR L 193 88.275 107.284 213.386 1.00 53.74 ATOM 5695 CE1 TYR L 193 89.329 107.696 212.587 1.00 56.34 ATOM 5696 CZ TYR L 193 89.239 107.563 211.211 1.00 56.42 ATOM 5697 OH TYR L 193 90.281 107.969 210.402 1.00 53.26 ATOM 5698 CE2 TYR L 193 88.104 107.026 210.637 1.00 51.05 ATOM 5699 CD2 TYR L 193 87.058 106.618 211.443 1.00 52.78 ATOM 5700 C TYR L 193 85.061 104.341 215.022 1.00 59.90 ATOM 5701 O TYR L 193 83.878 104.676 215.014 1.00 61.23 ATOM 5702 N ALA L 194 85.597 103.598 215.983 1.00 60.60 ATOM 5703 CA ALA L 194 84.781 103.023 217.040 1.00 60.44 ATOM 5704 CB ALA L 194 84.867 101.506 217.001 1.00 58.03 ATOM 5705 C ALA L 194 85.167 103.539 218.422 1.00 62.06 ATOM 5706 O ALA L 194 86.348 103.706 218.729 1.00 59.65 ATOM 5707 N CYS L 195 84.150 103.803 219.239 1.00 65.23 ATOM 5708 CA CYS L 195 84.334 104.113 220.647 1.00 64.15 ATOM 5709 CB CYS L 195 83.490 105.325 221.049 1.00 65.14 ATOM 5710 SG CYS L 195 83.565 105.667 222.813 1.00 76.11 ATOM 5711 C CYS L 195 83.926 102.893 221.471 1.00 64.61 ATOM 5712 O CYS L 195 82.788 102.427 221.382 1.00 64.34 ATOM 5713 N GLU L 196 84.854 102.374 222.269 1.00 64.38 ATOM 5714 CA GLU L 196 84.590 101.171 223.054 1.00 61.82 ATOM 5715 CB GLU L 196 85.634 100.096 222.768 1.00 62.01 ATOM 5716 CG GLU L 196 85.386 98.811 223.532 1.00 65.56 ATOM 5717 CD GLU L 196 86.560 97.862 223.468 1.00 72.33 ATOM 5718 OE1 GLU L 196 87.105 97.529 224.543 1.00 71.97 ATOM 5719 OE2 GLU L 196 86.940 97.457 222.347 1.00 69.46 ATOM 5720 C GLU L 196 84.540 101.459 224.548 1.00 62.08 ATOM 5721 O GLU L 196 85.537 101.858 225.152 1.00 62.10 ATOM 5722 N VAL L 197 83.368 101.244 225.137 1.00 64.72 ATOM 5723 CA VAL L 197 83.113 101.595 226.530 1.00 62.00 ATOM 5724 CB VAL L 197 81.862 102.484 226.647 1.00 62.70 ATOM 5725 CG1 VAL L 197 81.589 102.825 228.097 1.00 63.60 ATOM 5726 CG2 VAL L 197 82.027 103.751 225.816 1.00 66.14 ATOM 5727 C VAL L 197 82.906 100.357 227.399 1.00 62.52 ATOM 5728 O VAL L 197 82.273 99.391 226.972 1.00 62.84 ATOM 5729 N THR L 198 83.456 100.390 228.611 1.00 62.60 ATOM 5730 CA THR L 198 83.191 99.357 229.613 1.00 63.42 ATOM 5731 CB THR L 198 84.406 98.427 229.853 1.00 65.96 ATOM 5732 OG1 THR L 198 85.541 99.201 230.260 1.00 75.57 ATOM 5733 CG2 THR L 198 84.757 97.660 228.592 1.00 57.81 ATOM 5734 C THR L 198 82.757 100.000 230.930 1.00 64.10 ATOM 5735 O THR L 198 83.330 101.003 231.371 1.00 65.07 ATOM 5736 N HIS L 199 81.731 99.420 231.543 1.00 61.28 ATOM 5737 CA HIS L 199 81.128 99.979 232.743 1.00 61.88 ATOM 5738 CB HIS L 199 80.074 101.026 232.361 1.00 59.54 ATOM 5739 CG HIS L 199 79.401 101.675 233.532 1.00 60.06 ATOM 5740 ND1 HIS L 199 79.939 102.758 234.195 1.00 60.00 ATOM 5741 CE1 HIS L 199 79.125 103.122 235.172 1.00 58.26 ATOM 5742 NE2 HIS L 199 78.078 102.317 235.163 1.00 66.77 ATOM 5743 CD2 HIS L 199 78.223 101.406 234.145 1.00 56.76 ATOM 5744 C HIS L 199 80.503 98.859 233.570 1.00 62.31 ATOM 5745 O HIS L 199 80.210 97.778 233.052 1.00 62.64 ATOM 5746 N GLN L 200 80.305 99.126 234.856 1.00 63.07 ATOM 5747 CA GLN L 200 79.754 98.141 235.779 1.00 62.63 ATOM 5748 CB GLN L 200 79.880 98.651 237.215 1.00 62.52 ATOM 5749 CG GLN L 200 79.588 97.606 238.274 1.00 69.70 ATOM 5750 CD GLN L 200 79.649 98.173 239.675 1.00 69.60 ATOM 5751 OE1 GLN L 200 80.514 98.991 239.991 1.00 72.99 ATOM 5752 NE2 GLN L 200 78.728 97.739 240.524 1.00 71.95 ATOM 5753 C GLN L 200 78.295 97.810 235.466 1.00 61.35 ATOM 5754 O GLN L 200 77.801 96.742 235.824 1.00 62.32 ATOM 5755 N GLY L 201 77.610 98.731 234.797 1.00 61.85 ATOM 5756 CA GLY L 201 76.203 98.548 234.460 1.00 61.66 ATOM 5757 C GLY L 201 76.024 97.778 233.170 1.00 63.69 ATOM 5758 O GLY L 201 74.910 97.406 232.812 1.00 65.12 ATOM 5759 N LEU L 202 77.130 97.540 232.474 1.00 63.44 ATOM 5760 CA LEU L 202 77.118 96.790 231.227 1.00 63.71 ATOM 5761 CB LEU L 202 77.900 97.548 230.153 1.00 65.14 ATOM 5762 CG LEU L 202 77.491 99.011 229.958 1.00 65.05 ATOM 5763 CD1 LEU L 202 78.504 99.769 229.107 1.00 65.16 ATOM 5764 CD2 LEU L 202 76.094 99.099 229.354 1.00 68.62 ATOM 5765 C LEU L 202 77.723 95.409 231.433 1.00 63.71 ATOM 5766 O LEU L 202 78.803 95.276 232.009 1.00 63.14 ATOM 5767 N ARG L 203 77.021 94.381 230.963 1.00 65.26 ATOM 5768 CA ARG L 203 77.491 93.001 231.083 1.00 61.42 ATOM 5769 CB ARG L 203 76.321 92.009 231.027 1.00 62.44 ATOM 5770 CG ARG L 203 75.445 92.084 229.776 1.00 64.30 ATOM 5771 CD ARG L 203 74.254 93.019 229.974 1.00 75.27 ATOM 5772 NE ARG L 203 74.584 94.398 229.626 1.00 83.36 ATOM 5773 CZ ARG L 203 74.211 94.992 228.498 1.00 79.74 ATOM 5774 NH1 ARG L 203 73.478 94.334 227.610 1.00 88.38 ATOM 5775 NH2 ARG L 203 74.565 96.244 228.257 1.00 65.99 ATOM 5776 C ARG L 203 78.533 92.668 230.018 1.00 60.72 ATOM 5777 O ARG L 203 78.957 91.518 229.884 1.00 60.95 ATOM 5778 N SER L 204 78.938 93.684 229.264 1.00 58.82 ATOM 5779 CA SER L 204 79.984 93.543 228.261 1.00 61.63 ATOM 5780 CB SER L 204 79.502 92.684 227.089 1.00 63.29 ATOM 5781 OG SER L 204 78.884 93.482 226.092 1.00 66.85 ATOM 5782 C SER L 204 80.395 94.912 227.739 1.00 60.33 ATOM 5783 O SER L 204 79.615 95.863 227.806 1.00 60.22 ATOM 5784 N PRO L 205 81.625 95.019 227.212 1.00 61.02 ATOM 5785 CA PRO L 205 82.010 96.249 226.538 1.00 61.77 ATOM 5786 CB PRO L 205 83.375 95.911 225.919 1.00 61.00 ATOM 5787 CG PRO L 205 83.526 94.426 226.042 1.00 59.56 ATOM 5788 CD PRO L 205 82.710 94.024 227.216 1.00 61.93 ATOM 5789 C PRO L 205 81.006 96.592 225.445 1.00 62.47 ATOM 5790 O PRO L 205 80.459 95.698 224.795 1.00 67.71 ATOM 5791 N VAL L 206 80.769 97.881 225.253 1.00 62.93 ATOM 5792 CA VAL L 206 79.811 98.353 224.266 1.00 62.71 ATOM 5793 CB VAL L 206 78.620 99.078 224.958 1.00 62.90 ATOM 5794 CG1 VAL L 206 78.191 100.316 224.194 1.00 48.37 ATOM 5795 CG2 VAL L 206 77.457 98.111 225.141 1.00 64.78 ATOM 5796 C VAL L 206 80.503 99.240 223.226 1.00 64.33 ATOM 5797 O VAL L 206 81.299 100.117 223.568 1.00 61.76 ATOM 5798 N THR L 207 80.211 98.987 221.954 1.00 64.08 ATOM 5799 CA THR L 207 80.856 99.704 220.861 1.00 62.02 ATOM 5800 CB THR L 207 81.465 98.728 219.832 1.00 62.27 ATOM 5801 OG1 THR L 207 82.233 97.724 220.506 1.00 66.79 ATOM 5802 CG2 THR L 207 82.358 99.470 218.851 1.00 64.65 ATOM 5803 C THR L 207 79.888 100.626 220.126 1.00 59.75 ATOM 5804 O THR L 207 78.805 100.207 219.717 1.00 59.72 ATOM 5805 N LYS L 208 80.285 101.883 219.965 1.00 54.29 ATOM 5806 CA LYS L 208 79.597 102.796 219.065 1.00 52.66 ATOM 5807 CB LYS L 208 79.096 104.031 219.817 1.00 54.20 ATOM 5808 CG LYS L 208 77.725 103.855 220.448 1.00 57.19 ATOM 5809 CD LYS L 208 76.622 103.923 219.405 1.00 66.40 ATOM 5810 CE LYS L 208 75.247 103.760 220.037 1.00 76.46 ATOM 5811 NZ LYS L 208 74.157 103.851 219.022 1.00 77.59 ATOM 5812 C LYS L 208 80.569 103.204 217.972 1.00 53.19 ATOM 5813 O LYS L 208 81.684 103.639 218.261 1.00 55.00 ATOM 5814 N SER L 209 80.156 103.059 216.717 1.00 53.66 ATOM 5815 CA SER L 209 81.049 103.342 215.603 1.00 54.54 ATOM 5816 CB SER L 209 81.804 102.078 215.204 1.00 56.11 ATOM 5817 OG SER L 209 80.911 101.095 214.711 1.00 50.55 ATOM 5818 C SER L 209 80.331 103.911 214.385 1.00 58.17 ATOM 5819 O SER L 209 79.101 103.928 214.322 1.00 58.19 ATOM 5820 N PHE L 210 81.120 104.373 213.419 1.00 59.51 ATOM 5821 CA PHE L 210 80.594 104.875 212.157 1.00 61.61 ATOM 5822 CB PHE L 210 80.240 106.361 212.262 1.00 60.27 ATOM 5823 CG PHE L 210 81.430 107.262 212.458 1.00 61.97 ATOM 5824 CD1 PHE L 210 81.832 107.636 213.732 1.00 63.20 ATOM 5825 CE1 PHE L 210 82.922 108.470 213.915 1.00 62.86 ATOM 5826 CZ PHE L 210 83.623 108.945 212.819 1.00 65.33 ATOM 5827 CE2 PHE L 210 83.230 108.583 211.541 1.00 61.33 ATOM 5828 CD2 PHE L 210 82.138 107.749 211.366 1.00 62.59 ATOM 5829 C PHE L 210 81.603 104.657 211.040 1.00 63.34 ATOM 5830 O PHE L 210 82.804 104.534 211.293 1.00 63.38 ATOM 5831 N ASN L 211 81.106 104.604 209.807 1.00 66.16 ATOM 5832 CA ASN L 211 81.959 104.517 208.630 1.00 66.57 ATOM 5833 CB ASN L 211 81.288 103.672 207.547 1.00 69.08 ATOM 5834 CG ASN L 211 81.067 102.235 207.981 1.00 73.26 ATOM 5835 OD1 ASN L 211 81.683 101.760 208.941 1.00 77.79 ATOM 5836 ND2 ASN L 211 80.185 101.532 207.273 1.00 70.73 ATOM 5837 C ASN L 211 82.268 105.908 208.091 1.00 67.45 ATOM 5838 O ASN L 211 81.358 106.695 207.830 1.00 67.11 ATOM 5839 N ARG L 212 83.553 106.208 207.931 1.00 68.90 ATOM 5840 CA ARG L 212 83.987 107.536 207.499 1.00 71.51 ATOM 5841 CB ARG L 212 85.508 107.587 207.363 1.00 70.59 ATOM 5842 CG ARG L 212 86.077 108.981 207.467 1.00 66.81 ATOM 5843 CD ARG L 212 87.414 109.109 206.773 1.00 70.17 ATOM 5844 NE ARG L 212 87.264 109.580 205.399 1.00 81.63 ATOM 5845 CZ ARG L 212 87.371 108.808 204.323 1.00 79.09 ATOM 5846 NH1 ARG L 212 87.636 107.516 204.454 1.00 91.84 ATOM 5847 NH2 ARG L 212 87.216 109.330 203.115 1.00 84.00 ATOM 5848 C ARG L 212 83.341 107.956 206.180 1.00 75.77 ATOM 5849 O ARG L 212 83.233 107.156 205.246 1.00 75.19 ATOM 5850 N GLY L 213 82.919 109.216 206.112 1.00 78.54 ATOM 5851 CA GLY L 213 82.317 109.767 204.900 1.00 84.82 ATOM 5852 C GLY L 213 81.113 108.977 204.423 1.00 88.05 ATOM 5853 O GLY L 213 81.048 108.563 203.263 1.00 88.69 ATOM 5854 N GLU L 214 80.159 108.769 205.326 1.00 91.58 ATOM 5855 CA GLU L 214 78.954 108.008 205.021 1.00 94.24 ATOM 5856 CB GLU L 214 79.278 106.516 204.934 1.00 94.02 ATOM 5857 CG GLU L 214 78.264 105.698 204.152 1.00 94.64 ATOM 5858 CD GLU L 214 78.693 104.255 203.978 1.00 93.42 ATOM 5859 OE1 GLU L 214 79.267 103.683 204.929 1.00 89.65 ATOM 5860 OE2 GLU L 214 78.455 103.691 202.889 1.00 93.02 ATOM 5861 C GLU L 214 77.904 108.254 206.098 1.00 96.68 ATOM 5862 O GLU L 214 78.242 108.547 207.247 1.00 97.38 ATOM 5863 N CYS L 215 76.632 108.142 205.726 1.00 99.14 ATOM 5864 CA CYS L 215 75.542 108.334 206.679 1.00 101.74 ATOM 5865 CB CYS L 215 75.176 109.820 206.799 1.00 102.55 ATOM 5866 SG CYS L 215 74.364 110.563 205.351 1.00 108.00 ATOM 5867 C CYS L 215 74.311 107.502 206.326 1.00 101.45 ATOM 5868 O CYS L 215 73.500 107.178 207.197 1.00 101.05 ATOM 5869 OXT CYS L 215 74.102 107.129 205.170 1.00 100.37

The present disclosure also provides for a machine-readable data storage medium which comprises a data storage material encoded with machine readable data defined by the structure coordinates of a stabilized gp120 polypeptide as define in Table 1, or a subset thereof, such as at least about 5, such at least about 10, at least about 20, at least about 30, at least at least about 40, at least about 50, at least about 60, at least about 70, at least about 80, at least about 90, at least about 100, at least about 150, at least about 200, at least about 250, at least about 300, at least about 350, at least about 400, at least about 450, at least about 500 or more atoms of the structure, such as defined by the coordinates of Table 1.

In some examples, the coordinates provided are the coordinates of residues in contact with the neutralizing antibody b12, such as the coordinates of methionine 475, isoleucine 371, aspartic acid 474, glycine 366, asparagine 386, threonine 373, proline 369, glycine 367, arginine 419, aspartic acid 368, serine 365, glycine 473, asparagine 280, threonine 455, a subset of these coordinates, such as the atoms in contact with b12 as shown in FIGS. 5A-5D, those in contact with b12 CDR1 those in contact with b12 CDR2, those in contact with b12 CDR3, the CD4 loop or a combination thereof.

Those of skill in the art will understand that a set of structure coordinates for a gp120 polypeptide, for example a stabilized gp120 polypeptide, or a stabilized gp120 polypeptide in complex with an antibody, for example a neutralizing antibody such as the b12 antibody, or a portion thereof, is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape. Moreover, slight variations in the individual coordinates will have little effect on overall shape. The variations in coordinates discussed above may be generated because of mathematical manipulations of the structure coordinates. For example, the structure coordinates set forth in Table 1, or a portion thereof could be manipulated by crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates; integer additions or subtractions to sets of the structure coordinates, deletion of a portion of the coordinates, inversion of the structure coordinates, or any combination of the above.

This disclosure further provides systems, such as computer systems, intended to generate structures and/or perform rational drug or compound design for an antigenic compound capable of eliciting an immune response in a subject. The system can contain one or more or all of: atomic coordinate data according to Table 1, or a subset thereof; and the Figures derived therefrom by homology modeling, the data defining the three-dimensional structure of a gp120 or at least one sub-domain thereof, or structure factor data for gp120, the structure factor data being derivable from the atomic coordinate data of Table 1 or a subset thereof and the Figures. The disclosure also involves computer readable media with: atomic coordinate data according to Table 1 or a subset thereof and/or the Figures or derived therefrom by homology modeling, the data defining the three-dimensional structure of a gp120 or at least one sub-domain thereof; or structure factor data for a gp120, the structure factor data being derivable from the atomic coordinate data of Table 1, or a subset thereof and/or the Figures. By providing such computer readable media, the atomic coordinate data can be routinely accessed to the gp120 or a sub-domain thereof. For example RASMOL (Sayle et al., TIBS vol. 20 (1995), 374) is a publicly available software package which allows access and analysis of atomic coordinate data for structural determination and/or rational drug design. Structure factor data, which are derivable from atomic coordinate data (see, for example, Blundell et al., in Protein Crystallography, Academic Press, NY, London and San Francisco (1976)), are particularly useful for calculating electron density maps, for example, difference Fourier electron density maps. Thus, there are additional uses for the computer readable media and/or computer systems and/or atomic coordinate data and additional reasons to provide them to users.

VII. Identification of Immunogens

The crystals of the disclosure and particularly the atomic structure coordinates obtained from these crystals are particularly useful for identifying compounds that elicit neutralizing antibodies, for example CD4BS antibodies. The compounds identified are useful in eliciting antibodies to gp120, such as antibodies to lentivirus, such as SW, or HIV, for example HIV-I or HIV-II.

The crystal structure of a stabilized form of gp120 in complex with the b12 antibody allows a novel approach for drug or compound discovery, identification, and design of compounds that mimic the antigenic surfaces of gp120 that bind neutralizing antibodies, for example CD4BS antibodies such as b12. Such compounds can be useful as immunogens to elicit an immune response to HIV when administered to a subject, for example by eliciting anti-HIV antibodies, such as neutralizing antibodies, for example CD4BS antibodies. Compounds that elicit anti-HIV antibodies are useful in diagnosis, treatment, or prevention of HIV-I in a subject in need thereof.

The disclosure provides a computer-based method of rational drug or compound design, or identification which comprises: providing the structure of a stabilized form of gp120 (for example as defined by the coordinates or a subset of the coordinates in Table 1 and/or in the Figures); providing a structure of a candidate compound; and fitting the structure of the candidate compound to the structure of the stabilized form of gp120 (for example as defined by the coordinates or a subset of the coordinates in Table 1 and/or in the Figures).

In certain embodiments, the coordinates of atoms of interest of the stabilized form of gp120 in the vicinity of the antigenic surface are used to model the antigenic surface to which as antibody binds, such as a neutralizing antibody, for example a CD4BS antibody. These coordinates may be used to define a space which is then screened “in silico” against a candidate compound. Thus, this disclosure provides a computer-based method of rational drug or compound design or identification which comprises: providing the coordinates of at least two atoms of Table 1; providing the structure of a candidate compound; and fitting the structure of the candidate to the coordinates of at least two atoms of Table 1.

In practice, it may be desirable to model a sufficient number of atoms of the stabilized form of gp120 as defined by the coordinates of Table 1 which represent the binding region of interest, such as an antigenic surface. Thus, there can be provided the coordinates of at least about 5, such at least about 10, at least about 20, at least about 30, at least at least about 40, at least about 50, at least about 60, at least about 70, at least about 80, at least about 90, at least about 100, at least about 150, at least about 200, at least about 250, at least about 300, at least about 350, at least about 400, at least about 450, or at least about 500 atoms of the structure. In some examples, it may be advantageous to provide the coordinates of residues in contact with the neutralizing antibody b12, such as the coordinates of methionine 475, isoleucine 371, aspartic acid 474, glycine 366, asparagine 386, threonine 373, proline 369, glycine 367, arginine 419, aspartic acid 368, serine 365, glycine 473, asparagine 280, threonine 455, a subset of these coordinates, such as the atoms in contact with b12 as shown in FIGS. 5A-5D. FIGS. 5A-5D show specific contacts made between b12 and a stabilized form of g120. Atoms of gp120 that participate in these contacts can thus be provided to represent a binding region of interest. For example, one can model the coordinates in contact with b12 CDR1 those in contact with b12 CDR2, those in contact with b12 CDR3, the CD4 loop or a combination thereof. In some examples, it may be advantageous to provide the coordinates of residues that are buried as a result of gp120 contacting b12. For example, the using the program MS (Connolly Science, 221, 709-713, 1983) the surface (atomic coordinates) of the gp120 excluded form contact with solvent by b12 binding can be determined. Thus, the atomic coordinates of this surface can be provided to model an antigenic surface. In one example, the surface is defined by the residues listed in Table 3 or a subset thereof. In other examples, visual inspection of a computer generated representation of the atomic coordinates provides the residues of a stabilized gp120 in contact with b12. For example, one of ordinary skill in the art can use the program RASMOL (Sayle et al., TIBS vol. 20 (1995), 374) to determine the atoms of gp210 in contact with the b12 antibody and these atoms can be used to define an antigenic surface.

The disclosed methods can employ a sub-domain, region, or fragment of interest of the stabilized form of gp120 which is in the vicinity of the antigenic surface, and providing a computer-based method for identifying or rationally designing a compound or drug, such as an immunogen which includes: providing the coordinates of at least a sub-domain, region, or fragment of the stabilized form of gp120; providing the structure of a candidate compound that mimics the antigenic surface of the stabilized form of gp120; and fitting the structure of the candidate compound to the coordinates of the stabilized form of gp120 sub-domain, region, or fragment provided. A “sub-domain,” “region,” or “fragment” can mean at least one, for example, one, two, three, four, or more, element(s) of secondary structure of particular regions of the stabilized form of gp120, and includes those set forth in Table 1.

These methods can optionally include synthesizing the candidate compound, (such as an immunogen) and/or administering the candidate compound to an animal capable of eliciting antibodies and testing whether the candidate compound elicits anti-HIV antibodies. Compounds which elicit anti-HIV antibodies are useful for diagnostic purposes, as well as for immunogenic, immunological or even vaccine compositions, as well as pharmaceutical compositions.

In some embodiments, the candidate compound is designed from the gp120 amino acid sequence, for example an amino acid sequence is assembled to provide a candidate compound, for example by synthesizing the amino acid sequence or producing a nucleic acid encoding the candidate compound.

The step of providing the structure of a candidate compound may involve selecting the candidate compound by computationally screening a database of compounds for surface similarity with an epitope on the stabilized form of gp120. For example, a 3-D descriptor for the candidate compound may be derived, wherein the descriptor includes geometric and functional constraints derived from the architecture and chemical nature of the epitope. The descriptor may then be used to interrogate the compound database, a candidate compound being a compound that has a good match to the features of the descriptor. In effect, the descriptor can be a type of virtual pharmacophore.

By way of example, a compound that potentially mimics the antigenic surface of the stabilized form of gp120 can be examined through the use of computer modeling using a docking program such as GRAM, DOCK or AUTODOCK (see for example, Walters et al. Drug Discovery Today, 3(4):160-178, 1998; Dunbrack et al. Folding and Design 2:27-42, 1997). This procedure can include computer fitting of potential immunogens to ascertain how well the shape and the chemical structure of the potential immunogen will mimic the antigenic surface. Various other computer programs such as AMBER or CHARM may be used to further refine the dynamic and electrostatic characteristics of a candidate compound. Programs such as GRID (Goodford, J. Med. Chem, 28:849-57, 1985) may also be used to analyze the antigenic surfaces to predict immunogenic compounds. Alternatively, computer-assisted, manual examination can be used to predict immunogenic compounds from antigenic surfaces.

VIII. Stabilized gp120 Polypeptides as Crystallization Tools

One problem with the formation of crystals containing wild-type gp120 is that conformationally variable molecules are not amenable to crystallization. For an ordered crystal to form the molecules forming the crystal must be substantially locked in place. Molecules that are unstable or “floppy” such as wild-type gp120 must overcome large entropic (ΔS) costs to form a crystal lattice. By using conformationally stabilized forms of gp120 this entropic cost of becoming ordered is lessened and crystals form more easily. This problem has been overcome, as disclosed herein, by crystallizing their complex of interest with a stabilized form of gp120. For example, stabilized forms of gp120 can be used to crystallize previously uncrystallizable broadly neutralizing antibodies. In one embodiment, the broadly neutralizing antibody does not induce conformational stabilization as measured by TΔS of less than 28 kcal/mol upon antibody binding to gp120. The use of broadly neutralizing antibodies is disclosed, for example, in Burton, Nature Reviews 2:706-713, 2002, herein incorporated by reference. One example of how this can be accomplished is by forming complexes of a stabilized form of gp120 and the antibody of interest in the presence of CD4.

The following examples are provided to illustrate certain particular features and/or embodiments. These examples should not be construed to limit the invention to the particular features or embodiments described.

EXAMPLES Example 1 Structure-Assisted Stabilization of gp120 in its CD4-Bound Conformation

This example describes the methods used to design stabilized forms of gp120 disclosed herein.

Characterization of ligands and antibodies that bind to the CD4-binding site of gp120 has been complicated by conformational flexibility. This flexibility was initially suggested by thermodynamic analysis of the CD4 interaction with gp120 (Myszka et al., Proc Natl Acad Sci U S A. 97(16):9026-31, 2000). The CD4-bound state of gp120 consists of an inner domain (containing the N and C termini), an outer domain, and a four-stranded bridging sheet minidomain. Two-thirds of the CD4 contact surface is with the outer domain, the remaining one-third with the bridging sheet. In the unliganded state, the inner domain is radically altered, with most of its secondary structural elements repositioned. The bridging sheet is pulled apart with the two β-hairpins of the sheet separated by 20 Å. The outer domain, by contrast, remains virtually unchanged.

To stabilize gp120 into its CD4-bound conformation, an iterative-structure-based scheme was employed to construct interdomain disulfides and cavity-filling mutations (FIG. 1) including: (1) crystallographic determination of the gp120 mutant structure (2) isothermotitration calorimetric analysis of the entropy of CD4 binding, and (3) precise surface-plasmon resonance analysis of the on/off rates of antibodies to the modified gp120 glycoproteins.

Alteration of an unusual interfacial pocket at the nexus of the inner domain, outer domain and bridging sheet previously identified a S375W mutant that appeared to partially stabilized gp120 in its CD4-bound conformation (Xiang et al., J. Virol. 76(19):9888-99, 2002). This mutant was found to be difficult to handle biochemically. An additional T257S change, however, les to a well-behaved protein, and the structure of a S375W, T257S gp120 core bound to CD4 and Fab 17b was solved at 2.0 Å resolution (FIG. 1, FIG. 10 (supplemental Table 1)).

Cα carbon distances were analyzed to construct novel interdomain disulfides within the context of the S375W, T257S structure. Molecular modeling suggested four interdomain disulfides, connecting residues: 96-275, 109-428, 231-267 and 231-268. The disulfide at residue 96 was achieved by a Trp to Cys change. However this creates a large cavity; and an additional M95W change was introduced to compensate. All four disulfide combinations were constructed in the context of the S375W, T257S core. In addition, a 123-431 disulfide that tied together the second and third strands of the bridging sheet as well as an A433M cavity-filling alteration also were tested. Structural analysis in the context of CD4 and Fab 17b at 2.0-2.2 Å resolution showed that four of these single disulfides formed (all except for 231-268), and that both M95W and A433M in the context of the 96-275 disulfide induced minimal structural perturbation (FIG. 1, FIG. 10 (supplemental Table 1)). Each of the four disulfides was structurally incompatible with the conformation of the unliganded SIV gp120 (FIG. 1B and Table 2).

TABLE 2 Relative disulfide distances in the CD4-bound conformation and in the unliganded SIV conformation. Cα-Cα Cα-Cα Category HIV Mutation SIV Equivalent Distance (Å) Distance (Å) Category HIV Mutation SIV Equivalent HIV SIV S-S  96-275  78-290 6.4 21.9 S-S 109-428  91-441 6.1 16.2 S-S 123-431 105-444 4.4 23.5 S-S 231-267 245-282 6.0 16.8 Cavity 257/375 271/391 5.2 5.6

To increase stabilization, disulfide and cavity filling combinations were tested (FIG. 11, supplemental Table 2). Folding difficulties were encountered with combinations of three or four interdomain disulfides. A four disulfide stabilized core did not fold, and only one combination of three disulfides produce adequate levels of folded protein (FIG. 1, FIG. 11 (supplemental Table 2)). This three disulfide variant with linkages at 96-275, 109-428, and 123-431 bound to CD4 and 17b at 2.8 Å resolution was analyzed. A two disulfide variant with linkages at 96-275, 109-428 at 2.5 Å resolution was also analyzed. In both structures, all interdomain disulfides formed.

Because the structures were determined in the presence of stabilizing ligand, the conformational flexibility in the unliganded state could not be determined. To measure the degree of conformational fixation, the effect of the various alterations on the entropy of interaction between stabilized gp120 and CD4 was assessed (FIG. 10 (supplementary Table 1), FIG. 11 (supplemental Table 3)). Cavity-filling mutants had little effect. Single disulfides tethering the center two strands of the bridging sheet (123-431) or the termini-proximal ends of the inner and outer domains (96-275 or 261-267) reduced the entropy of interaction by about 15-30%. A more substantial effect (60% reduction) was observed with a disulfide tethering the bridging sheet to the inner domain (109-428). Additional disulfides did not reduce further the entropy of CD4 interaction.

Example 2 Determination of the On-Rates of CD4 Induced Antibodies

This example describes the binding of various CD4 induced antibodies to stabilized forms of gp120 disclosed herein using qualitative biacore analysis.

Another procedure to access conformational stabilization was with CD41 antibodies. Because the epitope for CD4i-antibodies is only present in the CD4-bound conformation of gp120, the on-rate of CD4i-antibodies can also be used to assess the degree that a particular gp120 is stabilized in the CD4-bound conformation. The on-rates of the prototypic CD4i antibody, 17b, as well as an X5 derivative, m6, selected to bind HXBc2 strain were tested. The stabilized gp120 cores showed a variety of on-rates for 17b and m6, with the most extreme change for the three disulfide variant, a 95-fold increase in on-rate for 17b and a 65-fold increase for m6 versus WT (FIG. 10 (supplementary Table 1)).

The relationship between entropy and conformational change is complex; some CD4-mimetics, for example, induce only half the entropic change as CD4, but the same gp120 conformation (Huang et al., Structure 13(5):755-68, 2005). Nonetheless, reasonable correlations were observed between the on-rate for CD4i antibodies and the entropy of CD4 binding (FIG. 1C). Together, the results show that some of the stabilized gp120 were substantially, though not entirely, fixed in the CD4-bound conformation, with the 3-disulfide variant the most stabilized.

Surface-plasmon resonance (SPR) experiments were performed on a Biacore biosensor system at 25 C. Antibody (17b or m6 for the CD4i antibodies; F105, b12, 1.5e, etc. for CD4BS antibodies; b3, b3, b11 etc. for Fab fragments of CD4BS antibodies; and 2-domain CD4 for CD4) were immobilized on research grade CM5 sensor chips using the recommended standard amine coupling. Binding experiments were carried out in HBSP buffer (10 mM HEPES, pH 7.4, 150 mM NaCl and 0.005% surfactant P-20).

During the association phase, gp120 were passed over the buffer-equilibrated chip surface at a rate of 30 ul/min. After the association phase, bound analytes were allowed to dissociate for 5 min. The chip surface was then regenerated by two 25 ul injections of 10 mM Glycine/HCl (pH 3.0) at a flow rate of 50 ul/min. Association and dissociation values were calculated by numerical integration and global fitting to a 1:1 interaction model using BIAevaluation 3.0 software (Biacore, Inc.)

Example 3 Effect of Conformational Stabilization on CD4 and CD4-Binding Site Antibodies

The example describes the binding of CD and several CD4BS antibodies to the stabilized forms of gp120 disclosed herein.

The creation of gp120 variants stabilized in the CD4-bound conformation allowed the conformation change and CD4 engagement to be determined. In light of the large conformational change observed for CD4 binding, it was expected that, like 17b and m6, conformational stabilization would substantially increase the on-rate of CD4. However, almost no change in on-rate was observed (FIG. 1D, FIG. 12 (supplementary Table 4)). A change in off-rate was observed, resulting in an overall increase in affinity between WT core and 3-disulfide stabilized core of 27-fold. The kinetic data indicated that the initial contact surface recognized by CD4 was present prior to the CD4-induced conformational change. Conformational change is thus not required to expose an initial site of contact; rather it serves to lock CD4 into place, once contact has been made.

The effect of gp120 stabilization on a number of antibodies that recognized the CD4-binding site also was examined (FIG. 11 (supplementary Table 1), FIG. 12 (supplementary Table 4)). Binding to virtually all such monoclonal antibodies was greatly diminished by conformational stabilization, demonstrating the degree to which conformational change successful hides the CD4-bound conformation of the CD4-binding site from humoral immune recognition. Of the CD4-binding site antibodies tested, only the unique broadly neutralizing antibody, b12 bound with surprisingly superior affinity to gp120 stabilized in the CD4-bound conformation.

In the core context, each single interdomain disulfide reduced the entropy of CD4 interaction by roughly 10 kcal/mol, as measured by isothermotitration calorimetry (ITC). Combinations of disulfides were tested. Two disulfide combinations showed similar antigenic phenotypes suggesting a partially stabilized gp120 conformation; ITC analysis for several of the different two disulfide combinations showed the entropy of CD4 interaction was reduced by roughly 20 kcal/mol. Combinations of three and four disulfides were also tested, although most of these only expressed poorly, perhaps due to complications of folding so many cysteines into the correct disulfide bonds. Removal of additional core disulfide (such as the second conserved disulfide in the V1/V2 region) and stabilization of the V3 region may enhance folding. A summary of the qualitative Biacore and ITC results for 17 mutants is shown in Table 3.

TABLE 3 Qualitative BIACORE on Supernatant and ITC results Mutant Mutant location CD4/CD4i Name 257375 433 95W96275 109428 123431 231267 231268 CD4 7B M6 WT core* A A A C2 x AAA AA AA C2S5 x x AAA AA AA C2S2 x x A A nd C2S4 x x A A nd C2S3 x x A A nd C12 x x A A nd C123S1 x x x A A nd C2S24 x x x AA A nd C123S14 x x x x AA A nd C123S12 x x x x AA A nd C23S234 x x x x x A N N C2S234 x x x x A A A C123S124 x x x x x N N nd C12S134 x x x x A A A C123S134 x x x x x A N N C12S123 x x x x AA AA AAA C123S123 x x x x x A A A/N C123S1234 x x x x x A A A Mutant CD4BS DSC/TM CD4 entropy Name B12 F105 F91 15e m14 m18 SS folding deg, C. kcal/mol WT core* AA AA AA AA AA AA 0 FFFF 50.6 40 C2 AA N N A/N A/N AA 0 FFFF 50.6 43 C2S5 AA N N A/N A/N AA 0 FFFF 55.7 C2S2 A/N N N N N A 1 FFF 53.8 17 C2S4 AA N A/N N N AA 1 FFF 56.4 C2S3 A N N N N AA 1 FFF C12 A N N N N AA 1 FFF C123S1 AA N A N N AA 1 FFF 28 C2S24 N N N N N N 2 FFF 59.0 23 C123S14 A N N N N AA 2 F C123S12 A N N N N A/N 2 FF 19 C23S234 A/N N N N N N 3 F/N C2S234 A/N N N N N N 3 F/N C123S124 N N N N N N 3 N C12S134 A/N N N N N AA 3 F/N C123S134 A/N N N N N AA 3 F/N C12S123 A N N N N A/N 3 F C123S123 A N N N N A/N 3 F/N C123S1234 A N N N N N 4 F/N Qualitative biacore analysis and ITC of conformationally stabilized mutants. Biacore analyses were carried out on transfected cell supernatants or with purified protein at 10 ug/ml, “A” indicates binding, “F” indicates folding, and “N” indicates no binding or folding. The mutants are indicated with the wildtype residue and position followed by the substituted residue as follows, C1:M95W; C2:T275S/S375W; C3:A433M; S1:W96C/V275C; S2:I109C/Q428C; S3:T123C/G431C; S4K231C/E267C. For example, A433M means that a methionine has been substituted for an alanine to create a C3 mutant protein.

Example 4 Structure of b12 in Complex with a Stabilized gp120

This example describes the details of the b12 gp120 interaction at atomic resolution.

To facilitate a structural understanding of b12 interaction with gp120, the complex of gp120 and b12 was solved by X-ray crystallography. Previously, it has been shown that among receptor-binding site antibodies, b12 was unique in its ability to bind to gp120 without inducing conformational fixation. This lack of conformational fixation complicated crystallization of a b12:gp120 complex. By utilizing gp120 variants stabilized in the CD4-bound conformation, crystals of a complex of b12 with a two disulfide stabilized gp120 (96-275, 109-428 as well as M95W, T257S, S375W, and A433M (C123S12)) were obtained. Diffraction from these crystals extended to 2.3 Å. The structure was solved by molecular replacement using the Fab portion of the b12 structure. The initial molecular replacement allowed the outer domain of gp120 to be placed, and iterative refinement and model building allowed portions of the less ordered inner domain and bridging sheet to be defined.

The structure of b12 with gp120 is shown in FIG. 2. Only the heavy chain of b12 interacts with gp120. A total of 1324 Å² are buried in the interaction, 787 Å² on gp120 and 737 Å² of b12. These surface areas are in the range typical for antibody:protein interface, and about 30% larger than the surface buried by the CD41 antibodies, 17b or X5 (Kwong et al, Nature 393:648, 1998; Huang et al., Structure 13(5):755-68, 2005). Each of the three heavy chain complementarity-determining regions (CDRs) makes extensive contact. The CDR H1 (192 Å² contact surface) uses Arg 28 and Asn 31 to reach into the polar surface on the outer domain around β23 and β24 (FIG. 5A). The CDR H2 (245 Å² contact surface) uses Tyr 54 to grab onto one side of the protruding β15 (FIG. 5B). The CDR H3 (276 Å² contact surface) uses Tyr 102 to grab the other side of β15, and then extends a towards the glycosylated silent face, with Trp 104 at the CDR H3 tip stacking against the sidechain portions of an Arg and of N-linked glycosylated Asn 386 (FIG. 5C). Together, these five b12 heavy chain residues, at positions 28, 31, 53, 102 and 104, combine to make up 58% of the b12 contact surface. Mutation of any one of these residues to alanine ablates b12 binding.

In addition to the CDR loops, the heavy chain loop D-E also makes contacts (24 Å²). Minor interactions with framework regions, peripheral to the primary binding surface, are not uncommon.

The gp120 surface bound by b12 is virtually all on the gp120 outer domain. The outer domain is a stacked double barrel, covered at one end by the four turns of a helix. The gp120 surface contacted by b12 covers the face of the double barrel opposite the helix. On the upper barrel, contacts are made with loop D, β23 and β24. On the bottom barrel, contacts are made with the protruding β15/α3, as well as with β17 and β19. Peripheral contacts are also made with α20/β21, though this region is relatively disordered in the structure. Overall, the outer domain contacts comprise 82% of the gp120 contact surface with b12.

Example 5 Structural Comparison of gp120 in Unliganded, b12- and CD4-Bound States

This example describes the structural differences between the cd4 and b12 bound states of gp120.

The b12-bound conformation was quite similar to the CD4-induced one. The primary differences related to the bridging sheet and the region on the inner domain proximal to the bridging sheet. In the b12-bridging sheet, considerable rearrangement is observed between the b12-bound conformation and the unliganded and CD4-bound states. Of the four β-strands that make up the sheet, β2 and β3 are not ordered sufficiently to be resolved. Meanwhile, β20 proceeds directly from β19, so that the β20-β21 ribbon is turned 90° with respect to unliganded and CD4-bound conformations (FIG. 3B).

In the inner domain around the core N- and C-termini, the b12 conformation is different from the unliganded state and similar to the CD4-induced one. The 2 on 3 β-sandwich of the termini is retained, with a rigid body shift. The inner domain structural similarity is preserved through the first turn of the long α1 helix, and then breaks down. Despite a 109-428 disulfide and mutations at 257, 375 and 433 in this region, it is considerably different from both the unliganded and CD4-bound state. These differences may relate to movements of the inner domain required to accommodate access of the b12 CDR H2 loop. They demonstrate the flexibility of the inner domain and bridging sheet, even in the presence of multiple mutations designed to fix gp120 in the CD4-bound conformation.

Despite the outer domain being the central binding site for both b12 and CD4, its conformation is well preserved between unliganded, b12- and CD4-bound states (FIG. 3). Interestingly, the RMS deviation for residues of the outer domain in contact with b12 and CD4 is considerable higher, suggesting that the similarity in the outer domain is intrinsic to the domain, and not induced by b12 or CD4. The results highlight the flexibility of the bridging sheet and inner domain, and conformational stability of the outer domain.

Both CD4 and b12 bind primarily to the outer domain of gp120. However, their entropies of interaction are very different, with CD4 inducing 40-50 kcal/mol change, and b12 inducing only a 6 kcal/mol change. This difference in fixation of the overall gp120 structure can be seen directly in the divergent B-values induced in the domains. In the b12-induced conformation, only the outer domain is fixed (FIG. 4B). The average B-value of the outer domain was considerably the inner domain. By contrast, in the CD4-bound conformation, the outer and inner domains have similar overall B-values. (Some of the B-value fixation may relate to the 17b antibody binding, but the low entropy of 17b binding to the CD4-gp120 complex suggests that it is primarily CD4 that fixes conformation.) The angle of CD4 and b12 binding to gp120 is quite similar, especially for the contacting heavy chain.

The precise contact surface of CD4 and b12 on gp120 have considerable overlap (FIG. 4). Most of this overlap is on the outer domain, where the central focus of binding for both b12 and CD4 is b15 or the CD4-binding loop. The actual manner of contact between b12 and CD4 of the CD4-binding loop is quite different. b12 uses all three of its CDR heavy chain loops to grasp both sides of this loop, which accounts for 42% of the total contact surface of b12 with gp120. By contrast, CD4 only binds to one side of the loop, making antiparallel hydrogen-bonds to the mainchain (FIG. 4C).

There are also significant parallels between Tyr 53 of b12 and Phe 43 of CD4. Both of these aromatic residues bind to same side of the CD4-binding loop. The primary difference in b12 and CD4 contact with gp120 involves the bridging sheet. With b12, bridging sheet contacts are peripheral to the binding surface. Studies have shown that mutation of some b12-bridging sheet contact residues to alamine does not affect b12 binding. In contrast, with CD4, bridging sheet contacts are central to the binding surface. Studies have shown that mutation of CD4-bridging sheet contact residues to alanine ablates CD4 binding.

To further characterize the differences in binding between b12 and CD4, binding to a gp120 variant, termed “OD1” was determined. This variant consisted of residues 252-482: the entire outer domain and also V3 and two strands of the bridging sheet. Binding of b12 to OD1 showed nearly identical rates of association as to HXBc2 core gp120, though the dissociation rate was about 15-fold higher.

There was no observable interaction of OD1 to CD4, likely due to an extremely weak interaction. Because CD4 demonstrated little change in on-rate to the conformationally stabilized gp120s, the on-rate of OD1 to CD4 might still be similar to that of core, but there might be an extremely fast off-rate, limiting the inability to observe a CD4:OD1 interaction.

To compensate for the fast off-rate, a dodecameric variant of CD4 (Igatp-CD4) was used. Avidity provided by the multivalent binding of Igatp-CD4 serves to greatly reduce off-rate. Igatp-CD4 to bind to OD1 with an association rate only about 2-fold lower than the Igatp-CD4 on-rate to core gp120 was observed.

The results suggest the following scenario for b12 and CD4 interaction with gp120. Initial contact by CD4 occurs with the structurally invariant outer domain, on a surface constitutively exposed on the envelope spike. This interaction is not stable and CD4 readily falls off. However, at the cell-surface (or with dodecameric CD4) multiple CD4s can bind simultaneously to the viral spike and use avidity to enhance stability. The avidity-enhanced outer domain:CD4 complex provides a receptive contact surface for the bridging sheet. A highly coordinated rearrangement of the inner domain allows for formation of the bridging sheet, which welds CD4 into place.

Contact by b12 occurs at the same constitutively exposed surface initially recognized by CD4. However, b12 is able to latch onto this outer domain surface with high affinity, without additional conformational change. This lack of conformational constraint allows b12 to bind and neutralize primary isolates otherwise protected by conformational masking. In this manner, b12 utilizes the functionally conserved initial contact site for CD4 on gp120 to effectively neutralize HIV-1.

Example 6 Neutralization Breadth of b12

Although the surfaces of gp120 recognized by b12 and CD4 have considerable overlap, there are important differences in the precise amino acids recognized, in the conformations of the interacting surface, and in the relative strength of the b12 and CD4 interaction. The b12 binding epitope was segregated into four categories, which were defined based on differences or similarities in b12 and CD4 recognition. By using the large number of isolates whose b12 susceptibility and gp120 sequence have been characterized, the sequence variation of gp120 in each of the four recognition categories was calculated and correlated with b12 neutralization sensitivity.

Extension of the binding surface of b12 beyond the CD4 contact surface creates opportunities for gp120, and by extension HIV, to develop b12-resistance isolates. For example, the differential contacts made by CD4 and b12 on the CD4-binding loop of gp120 give HIV the opportunity to present mutations that disrupt b12 binding, but still maintain CD4 binding. This is exemplified by the P369L variants, highly prevalent with Clade C isolates, which are not bound to a significant extent by b12.

Example 7 Genomic Analysis of b12

The genomic origin and location of somatic mutations of b12 was analyzed. Overall, somatic mutations in the V and J genes of b12 account for 44 changes. This is 4 standard deviations greater than the average (23+/−5.5) number of somatic mutants observed for receptor-binding site antibodies (Huang, 2004), and such an unusual degree of somatic change might indicate selection difficulty. However, the light chain accounts for 23 of these changes, the heavy chain for 21, and not all of these changes are necessary for binding.

The b12 antibody was isolated from a phage display library, derived from the bone marrow of an HIV-I infected individual. Such libraries undergo heavy and light chain reassortment. As there are no light chain contacts with gp120, it was determined whether the light chain somatic changes were indirectly necessary. For the light chain residues with side-chain interactions with the heavy chain, some were altered by affinity maturation, but none of these changes were critical for light/heavy chain interactions.

In terms of the 21 heavy chain alterations, the total number of changes is not so unusual, with CD4i antibodies like X5 showing similar numbers of changes. However, three of the changes, S27N, T28R, and G52Y, were each essential for binding. The difficulty in acquiring all three of these mutations, reduces the likelihood that a b12 antibody would be elicited. The actual mode of b12 binding (to just the heavy chain) may result from addition geometric requirements related to insertion into the CD4 binding cavity. Such heavy chain only binding is also unusual.

Example 8 Calculation of Occluded Surface Area

The example details the atomic details of the surface of gp120 occluded from solvent by the binding of b12.

The molecular surface occluded from solvent was calculated with the program MS with a probe radius of 1.4 Å to approximate a water molecule (see Table 4).

TABLE 4 Surface occlusion calculated with MS 5685 ATOMS TRANSLATED FROM PDB FORMAT TO MS FORMAT 5685 ATOMS 0 OMITTED 0 COLLISION ONLY 5685 SURFACE SURFACE POINT DENSITY = 5.00000   PROBE RADIUS = 1.40000 BURIED SURFACE ONLY 76 NEIGHBORS MAXIMUM 40 YON AND 93 VICTIM PROBES 21 SADDLE AND 9 CONCAVE SURFACE POINTS REMOVED DURING NON- SYMMETRY ORSR 2828 CONTACT AND 2917 SADDLE AND 1203 CONCAVE SURFACE POINTS 6948 TOTAL SURFACE POINTS 208 ATOMS   6948 SURFACE POINTS    7 PIECES PIECE AREA VOLUME CENTER 1 669.891 54.826 98.735 138.530 270.919 2 7.665 1.665 94.104 149.683 260.265 3 59.690 9.702 110.539 134.709 263.435 4 660.339 3.269 98.622 137.462 270.110 5 67.904 1.450 109.017 134.599 262.829 6 13.173 −1.776 94.749 148.752 258.657 7 1.498 0.056 98.179 152.009 258.103 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 CHN RESI MAIN SIDE TOTAL 1 SURFACE AREA PIECE NUMBER 1 1 256 S 1.160 0.000 1.160 1 257 S 11.434 8.886 20.320 1 280 N 11.963 5.590 17.553 1 281 A 11.332 0.000 11.332 1 364 S 0.000 3.541 3.541 1 365 S 15.369 12.101 27.470 1 366 G 33.227 0.000 33.227 1 367 G 46.289 0.000 46.289 1 368 D 7.717 33.835 41.552 1 369 P 5.923 30.210 36.133 1 370 E 7.806 10.059 17.865 1 371 I 3.726 53.670 57.396 1 372 V 0.000 28.551 28.551 1 373 T 0.000 19.785 19.785 1 375 W 0.000 6.864 6.864 1 384 Y 9.758 4.001 13.759 1 386 N 7.326 24.801 32.127 1 417 P 5.424 10.631 16.055 1 418 C 6.827 0.000 6.827 1 419 R 2.275 45.443 47.718 1 453 L 0.000 3.357 3.357 1 455 T 0.000 30.602 30.602 1 456 R 11.442 0.000 11.442 1 457 D 3.061 2.064 5.125 1 458 G 1.510 0.000 1.510 1 470 P 0.817 0.000 0.817 1 471 G 1.367 0.000 1.367 1 472 G 24.261 0.000 24.261 1 473 G 34.815 0.000 34.815 1 474 D 16.923 8.915 25.838 1 475 M 15.719 29.521 45.240 SURFACE AREA PIECE NUMBER 2 1 281 A 0.000 7.665 7.665 1 SURFACE AREA PIECE NUMBER 3 1 430 V 10.969 9.443 20.412 1 431 G 9.957 0.000 9.957 1 432 K 0.000 29.321 29.321 1 SURFACE AREA PIECE NUMBER 4 2 28 R 0.000 65.254 65.254 2 30 S 0.000 17.633 17.633 2 31 N 24.004 42.144 66.148 2 32 F 4.118 31.751 35.869 2 33 V 3.687 8.146 11.833 2 52 N 0.000 14.101 14.101 2 53 P 5.757 0.000 5.757 2 54 Y 20.496 96.660 117.156 2 55 N 4.147 18.720 22.867 2 74 T 0.000 7.472 7.472 2 99 V 0.000 9.877 9.877 2 100 G 2.726 0.000 2.726 2 101 P 2.194 5.515 7.709 2 102 Y 17.389 67.332 84.721 2 103 S 3.070 0.000 3.070 2 104 W 18.039 97.955 115.994 2 105 D 2.639 0.928 3.567 2 106 D 3.231 0.000 3.231 2 108 P 5.838 12.394 18.232 2 109 Q 6.066 4.127 10.193 2 111 N 0.000 15.480 15.480 2 112 Y 0.000 21.458 21.458 1 SURFACE AREA PIECE NUMBER 5 2 50 W 0.000 14.761 14.761 2 55 N 0.000 0.385 0.385 2 57 N 3.242 33.908 37.150 2 58 K 12.150 0.000 12.150 2 59 E 0.000 2.464 2.464 2 109 Q 0.000 0.994 0.994 1 SURFACE AREA PIECE NUMBER 6 2 74 T 4.400 0.000 4.400 2 75 S 4.902 0.000 4.902 2 77 N 0.000 3.871 3.871 1 SURFACE AREA PIECE NUMBER 7 2 75 S 0.000 1.498 1.498 MAIN SIDE 1 SURFACE AREA PIECE NUMBER 1 A 11.332 0.000 C 6.827 0.000 D 27.701 44.814 E 7.806 10.059 G 141.469 0.000 I 3.726 53.670 L 0.000 3.357 M 15.719 29.521 N 19.289 30.391 P 12.164 40.841 R 13.717 45.443 S 27.963 24.528 T 0.000 50.387 V 0.000 28.551 W 0.000 6.864 Y 9.758 4.001 SURFACE AREA BY RESIDUE CLASS ACID 35.507 54.873 BASE 13.717 45.443 HYDROPHOBIC 42.941 162.804 POLAR 205.306 109.307 SURFACE AREA PIECE NUMBER 2 A 0.000 7.665 SURFACE AREA BY RESIDUE CLASS HYDROPHOBIC 0.000 7.665 SURFACE AREA PIECE NUMBER 3 G 9.957 0.000 K 0.000 29.321 V 10.969 9.443 SURFACE AREA BY RESIDUE CLASS BASE 0.000 29.321 HYDROPHOBIC 10.969 9.443 POLAR 9.957 0.000 SURFACE AREA PIECE NUMBER 4 D 5.870 0.928 F 4.118 31.751 G 2.726 0.000 N 28.151 90.445 P 13.789 17.909 Q 6.066 4.127 R 0.000 65.254 S 3.070 17.633 T 0.000 7.472 V 3.687 18.023 W 18.039 97.955 Y 37.885 185.450 SURFACE AREA BY RESIDUE CLASS ACID 5.870 0.928 BASE 0.000 65.254 HYDROPHOBIC 39.633 165.638 POLAR 77.898 305.127 SURFACE AREA PIECE NUMBER 5 E 0.000 2.464 K 12.150 0.000 N 3.242 34.293 Q 0.000 0.994 W 0.000 14.761 SURFACE AREA BY RESIDUE CLASS ACID 0.000 2.464 BASE 12.150 0.000 HYDROPHOBIC 0.000 14.761 POLAR 3.242 35.287 SURFACE AREA PIECE NUMBER 6 N 0.000 3.871 S 4.902 0.000 T 4.400 0.000 SURFACE AREA BY RESIDUE CLASS POLAR 9.302 3.871 SURFACE AREA PIECE NUMBER 7 S 0.000 1.498 SURFACE AREA BY RESIDUE CLASS POLAR 0.000 1.498

Example 9 Prime-Boost Immunization with Stabilized gp120 and gp140 Trimer

This example describes the “prime-boost” immunization scheme used to generate a heightened immune response in a subject.

Based on the biophysical characterization of gp120 stabilized in the CD4 bound conformation performed an immunization scheme was performed whereby HXBc2 strain wild-type or cysteine-stabilized core gp120 proteins were used to prime the immune response for subsequent immunization with soluble, stabilized trimeric YU2 strain gp140-foldon molecules (Yang et al. J Virol. 76(9):4634-42, 2002). B-cells primed by the stabilized cores were primed for epitopes displayed preferentially only on the stabilized HX core CD4 binding site, or to other stabilized surfaces, efficiently presented only by the cysteine-stabilized cores.

Boosting with the gp140 trimeric molecules “immuno-focuses” primed B cells on shared and conserved determinants between the two immunogens and altering strains would not boost B cells directed at HX- or YU2-specific epitopes. Thus, the only B-cells boosted selectively by the trimer would be those that could bind efficiently both the stabilized core as well as the trimer. Thus, stabilized cores can stimulate B cells that could induce the CD4-bound or the b12 conformation in the gp140 trimers.

Based upon this scheme, HIV gp120 core and trimer proteins were expressed by transient transfection of 293 cells with the relevant plasmid DNA. Soluble proteins were purified from culture supernatants by affinity chromatography and maintained in PBS, pH 7.4. Each rabbit was injected at two sites by the intramuscular route in the hind leg with 50 ug of protein emulsified at 1:1 ratio in GSK AS01B adjuvant in a total volume of 1 ml. The rabbits were inoculated four times with emulsified HX wild-type or stabilized core proteins followed by two injections with the emulsified YU2 gp140 trimeric proteins. Inoculations were performed at approximate four week intervals and the immune sera were collected ten days following each injection. The presence of high-titer anti-gp120 antibodies were confirmed by ELISA. The ability to neutralize viral particles derived from selected HIV strains was determined in a luciferase-based HIV entry assay. Virus was incubated with pre- or post-immune sera and the percent neutralization in the immune sera was calculated as the decrease in entry relative to virus incubated with pre-immune sera or an irrelevant BSA protein-emulsified control. The tabulated results of the immunogenicity-neutralization are shown in FIG. 4A-B.

Example 10 Conformational Masking of Stabilized Immunogens

This example describes the strategies to mask portions of a stabilized gp120 polypeptide from non-neutralizing antibodies.

The polypeptide “new 9c” as set forth as includes residues at the base of the V3 loop, and restores recognition of the core by the CD4-induced antibodies, such as 17b. Individual and combination glycan mutations were designed in the context of the stabilized gp120 polypeptides disclosed herein (for example, such as set forth in SEQ ID NO: 1) to prevent the elicitation of non-neutralizing antibodies. Using site-directed mutagenesis, specific Asn and Ser/Thr residues are incorporated into the 8b core. The Asn-X-Ser/Thr residues mediate the attachment of glycans to the designated asparagine residues by mammalian cell glycosylating enzymes in the endoplasmic reticulum. This scheme is used to mask the immunogenic but non-neutralizing surfaces present in gp120.

Typically, wild-type gp120 cores elicit antibodies in rabbits that bind more efficiently to the core proteins than to full length gp120 glycoproteins. It is likely that the cores, via their truncated loops and N- and C-termini, elicit antibodies to surfaces that are not exposed in monomeric gp120.

As another aspect of an overall strategy to optimize the stabilized core priming of a trimer boost, glycans are designed at selected densities on the stabilized core to dampen or eliminate unwanted core-specific responses based upon the 8b core-b12 structure disclosed herein. The optimized and proteins are expressed, purified, analyzed and tested for immunogenicity by themselves or in sequential prime-boost with the YU2 gp140 trimers.

To mask the surface recognized by 17b and other CD4-induced antibodies the following mutations were designed:

Mutation 1: Mutation 2

a. R419N: K421S b. I420N: Q422S c. Q422N: I424T d. I423N: N425T and one additional mutant to add 2 glycans e. R419N: K421S+I423N: N425T

To mask surfaces other than the CD4 binding site, which includes the b12 epitope region, the following N-glycan addition sites were designed:

Glycan Location Mutation 1 Mutation 2 1 246 Q246N 2 267 E267N E269T 3 97 K97N D99T 4 103 Q103N H105S 5 92 N94T 6 114 Q114N L116T 7 222 G222N A224T 8 201 I201N Q203T 9 206 P206N V208T 10  423 I423N N425T 11  434 M434N A436S 12  442 Q442N R444T 13  210 F210N P212T Density 2 1 246 Q246N 2 97 K97N D99T 3 103 Q103N H105S 4 201 I201N Q203T 5 206 P206N V208T 6 434 M434N A436S 7 442 Q442N R444T 8 210 F210N P212T 9 114 Q114N L116T Density 3 1 206 P206N V208T 2 442 Q442N R444T 3 114 Q114N L116T 4 246 Q246N 5 434 M434N A436S Mutation 1 and Mutation 2 correspond to the N glycosylation consensus sequence: NxT/S where x is anything except proline. T is better than S for glycosylation. Blanks indicate positions where no mutations are necessary. The glycosylated polypeptides can be used to induce an immune response in a subject.

Example 11 Identification of Immunogenic Fragments of gp120

This example describes the selection of immunogenic fragments of stabilized gp120.

A nucleic acid molecule encoding a stabilized p120 fragment is expressed in a host using standard techniques (see above; see Sambrook et al., Molecular Cloning; A Laboratory Manual, Cold Spring Harbor Press, Cold Spring Harbor, N.Y. 1989). Preferable gp120 fragment is expressed such that the gp120 fragment can be isolated or purified in sufficient quantity. The stabilized gp120 fragment that are expressed are analyzed by various techniques known in the art, such as immunoblot, and ELISA, and for binding to CD4 and mAbs directed to the CD4 binding site, for example the b12 antibody.

To determine the antigenic potential of stabilized p120 fragments, subjects such as mice, rabbits or other suitable subjects are immunized with stabilized p120 fragments. Sera from such immunized subjects are tested for antibody activity for example by ELISA with the expressed polypeptide. They are also tested in a CD4 binding assay, for example by qualitative biacore, and the binding of neutralizing antibodies, for example by using the b12 antibody. Thus antigenic fragments of stabilized forms are selected to archive broadly reactive neutralizing antibody responses.

Example 12 Detection of Antibodies with Similar Epitopes to B12

This example demonstrates how the antigenic surface of gp120 as defined by the interaction of gp120 and b12 can be used to detect b12-specific antibodies in sera obtained from a subject.

The g120 epitope that binds gp120 is grafted into lentivirus for example SIV or HIV, such as HIV-I or HIV-II, by site-directed mutagenesis. Suitable epitopes include the residues of gp120 in contact with b12, for example as defined by the structural coordinates of gp120 in complex with b12 as given in Table 2. For example the lentiviral construct can be engrafted with the residues in contact with b12 as set forth in FIG. 5A-FIG. 5D. The lentiviral epitope-engrafted variants are used as biological screens for the presence of neutralizing activity of these specificities.

In view of the many possible embodiments to which the principles of our invention may be applied, it should be recognized that the illustrated embodiment is only a preferred example of the invention and should not be taken as a limitation on the scope of the invention. Rather, the scope of the invention is defined by the following claims. We therefore claim as our invention all that comes within the scope and spirit of these claims. 

1. An isolated immunogen comprising a modified HIV-I gp120 polypeptide, or immunogenic fragment thereof, wherein the modified HIV-I gp120 polypeptide or immunogenic fragment thereof is stabilized in a CD4-bound conformation by mutationally introduced crosslinked cysteines consisting of residue pairs 96 and 275 and 109 and 428, and amino acid substitutions in the protein core at positions 95, 257, 375, and
 433. 2. The isolated immunogen according to claim 1, wherein the amino acid substitutions in the protein core comprise a methionine to tryptophan mutation at position 95 of gp120, a threonine to serine mutation at position 257 of gp120, a serine to tryptophan mutation at position 375 of gp120, an alanine to methionine mutation at position 433 of gp120, or a combination thereof.
 3. The isolated immunogen according to claim 1, comprising the amino acid sequence set forth as SEQ ID NO: 1, or immunogenic fragment thereof.
 4. The isolated immunogen according to claim 1, wherein the modified HIV-I gp120 polypeptide or immunogenic fragment thereof comprises the outer domain of the gp120 polypeptide.
 5. The isolated immunogen according to claim 4, wherein the outer domain comprises residues 109-246 and 261-299 of SEQ ID NO:
 1. 6. The isolated immunogen according to claim 5, wherein residues 246 and 261 of the outer domain are covalently linked.
 7. The isolated immunogen according to claim 5, wherein residues 246 and 261 of the outer domain are covalently linked by a peptide linker.
 8. The isolated immunogen according to claim 7, wherein the peptide linker comprises residues 247-260 of SEQ ID NO:
 1. 9. The isolated immunogen according to claim 1, wherein the immunogen is covalently linked to a carrier, Toll like receptor ligand, dendritic cell, or B cell targeting moiety.
 10. The isolated immunogen according to claim 1, wherein the immunogen is glycosylated.
 11. An isolated nucleic acid molecule comprising the nucleotide sequence encoding the polypeptide of claim
 1. 12. The isolated nucleic acid molecule of claim 11, comprising a nucleotide sequence encoding the polypeptide sequence set forth as SEQ ID NO:
 1. 13. The nucleic acid molecule of claim 12, operably linked to a promoter.
 14. A vector comprising the nucleic acid of claim
 13. 15. A host cell comprising the vector of claim
 14. 16. The host cell of claim 15, wherein the host cell is a mammalian host cell.
 17. The host cell of claim 16, wherein the host cell is a human host cell.
 18. A pharmaceutical composition comprising the isolated immunogen or an isolated nucleic acid molecule encoding the immunogen of claim 1 and a pharmaceutically acceptable carrier.
 19. A method for generating an immune response in a subject, comprising administering to the subject a therapeutically effective amount of the isolated immunogen or an isolated nucleic acid molecule encoding the immunogen of claim 1, thereby generating the immune response.
 20. The method of claim 19, further comprising administering a therapeutically effective amount of a polypeptide or nucleic acid molecule expressing a polypeptide comprising: a) monomeric or trimeric gp140 polypeptide; b) an unmodified monomeric or trimeric gp120 polypeptide; or c) any combination of a-b, above.
 21. A method for treating or preventing lentiviral infection in a subject, comprising administering to the subject a therapeutically effective amount of the isolated immunogen or an isolated nucleic acid molecule encoding the immunogen of claim 1, thereby treating the subject or preventing infection of the subject.
 22. The method of claim 21, wherein the lentivirus is a human immunodeficiency type 1 (HIV-1).
 23. The method of claim 21, further comprising administering a therapeutically effective amount of a polypeptide or nucleic acid molecule expressing a polypeptide comprising: a) monomeric or trimeric gp140 polypeptide; b) an unmodified monomeric or trimeric gp120 polypeptide; or c) any combination of a-b, above.
 24. The method of claim 22, further comprising administering to the subject a therapeutically effective amount of an additional at least one anti-human immunodeficiency virus (HIV) agent.
 25. The composition of claim 18 for use in inhibition of a human immunodeficiency virus (HIV) infection. 